CODSWALLOP

Poly(ethylene terephthalate) hydrolase

Piscinibacter sakaiensis · seed A0A0K8P6T7 · 290 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026

CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.

212Entries 213Entities 178Constructs 48Organisms 33Ligand-bound
0.89 ÅBest res.
1.61 ÅMedian res.

Every figure here is counted over the whole family rather than quoted from one entry.

The reference structure

8VEM, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.

Rendered structure of 8VEM
8VEM at the RCSB · open it in the 3D viewer

Which residues anyone has ever seen

How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.

1145290213 constructs

Constructs, most-used first

178 distinct constructs across 212 entries. 168 polymer entities differ from the UniProt canonical sequence in some way, 76 carry a recognised expression tag and 0 carry a fusion partner.

"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.

EntitiesLengthBest (Å)Best entryWhat was made
5 258 1.45 7CUV no UniProt reference for this entity, so it cannot be diffed against a canonical sequence
5 298 0.92 6EQE His6
4 260 1.38 8Z2I residues 45-304; Q45G, D46P, Q123H +7 more
4 263 1.10 7CTS residues 45-304; Q45G, D46P, Q123H +7 more
4 265 1.12 5ZRQ residues 43-304; T43G, A44P, S176A +2 more
3 258 1.38 7E31 no UniProt reference for this entity, so it cannot be diffed against a canonical sequence
3 260 1.10 8GZD residues 30-289
3 260 1.90 8JMP residues 34-293; A34G, Q35M, Y127G +4 more
3 262 1.20 5XH2 residues 29-290; T29M, R132G, S160A
3 273 1.45 4WFI residues 36-304; 1-residue insertion after 45; V36M, A37R, A39S +8 more
2 261 2.31 7XTV no UniProt reference for this entity, so it cannot be diffed against a canonical sequence
2 267 1.64 9RD2 His6; residues 35-293; Q35M, Y127G, D238C +2 more
2 267 1.70 8BRA matches the canonical sequence
2 272 2.02 6ANE His6; residues 27-290; A27M
2 282 1.40 4CG1 His6; residues 41-301; S58R, T176S
2 291 1.68 7VPB matches the canonical sequence
2 293 1.69 7VMD matches the canonical sequence
2 306 1.68 3WYN His6
1 254 1.75 9IW9 residues 41-292; 1 internal deletion; 2-residue insertion after 178; P41M, S43F, T45D +98 more
1 256 1.61 9XUE no UniProt reference for this entity, so it cannot be diffed against a canonical sequence
1 257 1.51 9QYU residues 36-292; L84Y, Y127G, D238C +2 more
1 257 1.64 9QYT residues 36-292; L84Y, Y127G, T144E +3 more
1 258 1.10 6THS residues 36-293; S165A
1 258 1.14 6THT residues 36-293; Y127G, S165A, D238C +2 more
1 258 1.50 4EB0 residues 36-293

Showing the 25 most-used of 178.

Positions people deliberately mutate

Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".

P60A 70% R90T 70% F229Y 70% I168R 69% A47R 69% T279P 69% A40E 69% G75S 69% Q133Y 69% Y63F 68% M128L 68% S290P 68% E274P 68% Y146R 68% R53A 68% S187T 68% V68I 68% I145V 67% T151P 67% S207T 66% I232L 66% K148R 66% G147S 65% S278D 65% S188D 65% S54T 65% V134L 65% V84S 64% A202G 63% N73D 63%

What it assembles into

Oligomeric stateChainsEntriesShare
monomeric1 203 95.8%
dimeric2 9 4.2%

76 entries have the depositor's assembly corroborated by PISA, 134 carry the depositor's word alone and 2 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 2 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 9JQW, 9LJ7.

Domain architecture

Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.

CATHAlpha/Beta hydrolase fold,SCOP2Balpha/beta-Hydrolasesalpha/beta-Hydrolasesalpha/beta-Hydrolasesalpha/beta-Hydrolasesalpha/beta-Hydrolases1145290
DomainSourceSpan (seed)Chains
Alpha/Beta hydrolase fold, catalytic domainCATH 3.40.50.1820 31–290 51
alpha/beta-HydrolasesSCOP2B 8103753 29–290 2
alpha/beta-HydrolasesSCOP2B 8085716 31–290 56
alpha/beta-HydrolasesSCOP2B 8094901 31–290 5
alpha/beta-HydrolasesSCOP2B 8085712 31–290 2
alpha/beta-HydrolasesSCOP2B 8085714 32–289 17

What binds it

C9C C9C7 entries J1K J1K4 entries NAG NAG4 entries PMS PMS2 entries UB7 UB72 entries NPO NPO1 entries 856 8561 entries 9J3 9J31 entries 9J6 9J61 entries 9YL 9YL1 entries LAC LAC1 entries PG0 PG01 entries
ComponentClassNameEntriesBest (Å)
GOLcryoprotectant Glycerol 40 1.12
SO4ion Sulfate Ion 36 1.12
CLion Chloride Ion 34 0.92
CAion Calcium Ion 31 1.09
EDOcryoprotectant 1,2-Ethanediol 24 1.08
NAion Sodium Ion 21 0.92
PEGcryoprotectant Di(Hydroxyethyl)ether 15 1.20
ACTcryoprotectant Acetate Ion 12 1.08
CITbuffer Citric Acid 9 1.12
MGion Magnesium Ion 8 1.38
C9Cligand 4-(2-Hydroxyethyloxycarbonyl)benzoic Acid 7 1.40
PG4cryoprotectant Tetraethylene Glycol 6 1.43
ZNion Zinc Ion 5 1.12
DIOcryoprotectant 1,4-Diethylene Dioxide 4 1.10
IMDbuffer Imidazole 4 1.14
J1Kligand 4-(2-Hydroxyethylcarbamoyl)benzoic Acid 4 1.68
NAGcofactor 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose 4 1.49
PO4ion Phosphate Ion 3 1.35
MPDcryoprotectant (4s)-2-Methyl-2,4-Pentanediol 3 1.40
PGEcryoprotectant Triethylene Glycol 3 1.38

How it crystallises

Parsed from the free text 208 depositors typed into _exptl_crystal_grow.pdbx_details, out of 209 entries that recorded anything at all. Median pH 6.5 (range 3.7 to 10.5).

Precipitants

PEG × Sodium chloride × Ammonium sulfate × Sodium citrate × MPD × PEG (unspecified) × Magnesium chloride × Sodium malonate × Calcium chloride × Isopropanol × Lithium sulfate × Jeffamine × Dioxane × Tacsimate ×

Buffers

Citrate × MES × Tris × HEPES × Bis-Tris × Sodium acetate × Bis-Tris propane × Imidazole × Sodium cacodylate × Phosphate × Glycine × CAPS ×

Which entries to trust

212 entries carry a wwPDB validation report: 184 clean, 28 worth a check and 0 with something to explain. Median clashscore 2.5, median RSRZ outliers 1.36%, median R-free minus R-work 0.031. 211 have released structure factors.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Pseudideonella sakaiensis56 0.92 8 100%
Saccharomonospora viridis18 1.09 7 89%
Thermobifida fusca13 1.08 3 85%
unidentified prokaryotic organism13 1.28 3 97%
uncultured bacterium12 1.10 0 90%
compost metagenome10 0.89 0 88%
unidentified10 1.30 6 90%
Cryptosporangium aurantiacum8 1.22 0 93%
synthetic construct7 1.42 0 90%
Rhizobacter gummiphilus4 1.08 0 98%
Thermomonospora curvata DSM 431834 1.10 1 88%
Thermobifida cellulosilytica4 1.45 0 85%

Seed sequence

290 residues, numbered every ten. Every identity figure in this document is measured against this sequence.

active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions

1MNFPRASRLM QAAVLGGLMA VSAAATAQTN PYARGPNPTA ASLEASAGPF TVRSFTVSRP
61SGYGAGTVYY PTNAGGTVGA IAIVPGYTAR QSSIKWWGPR LASHGFVVIT IDTNSTLDQP
121SSRSSQQMAA LRQVASLNGT SSSPIYGKVD TARMGVMGWS MGGGGSLISA ANNPSLKAAA
181PQAPWDSSTN FSSVTVPTLI FACENDSIAP VNSSALPIYD SMSRNAKQFL EINGGSHSCA
241NSGNSNQALI GKKGVAWMKR FMDNDTRYST FACENPNSTR VSDFRTANCS

Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.

Primary citations

One record per paper, not per entry.

YearCitation
2026 Computational engineering of the polyester hydrolase PHL7 for efficient poly(ethylene terephthalate) degradation in biocatalytic recycling processes. Nat Commun doi:10.1038/s41467-026-70868-4
2026 Cellular Upcycling of Polyethylene Terephthalate (PET) With an Engineered Human Saliva Metagenomic PET Hydrolase. Chemsuschem doi:10.1002/cssc.202502560
2026 Effect of surface electrostatic potential on pH-activity profile in PET depolymerases. J Hazard Mater doi:10.1016/j.jhazmat.2026.142179
2026 Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization. Nat Commun doi:10.1038/s41467-026-74839-7
2026 Development of a highly active engineered PETase enzyme for polyester degradation. Febs J. doi:10.1111/febs.70228
2025 Trade-Offs between Stability and Activity of Glycosylated and Non-Glycosylated Polyester Hydrolases PHL7 and PHL7mut3. Acs Es T Eng doi:10.1021/acsestengg.5c00272
2025 Landscape profiling of PET depolymerases using a natural sequence cluster framework. Science doi:10.1126/science.adp5637
2025 Enhancing the specificity of a thermostable PET hydrolase toward aromatic polyesters via Piscinibacter sakaiensis PETase-inspired mutations. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2025.149745
2025 Combined approaches to enhance the Pichia pastoris-expressed PET hydrolase. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2025.145862
2025 Functional and Structural Characterization of PETase SM14 from Marine-Sponge Streptomyces sp. Active on Polyethylene Terephthalate. Acs Sustain Chem Eng doi:10.1021/acssuschemeng.5c00737
2025 Application of a Rational Crystal Contact Engineering Strategy on a Poly(ethylene terephthalate)-Degrading Cutinase. Bioengineering (Basel) doi:10.3390/bioengineering12060561
2025 Ancestral reconstruction of polyethylene terephthalate degrading cutinases reveals a rugged and unexplored sequence-fitness landscape. Sci Adv doi:10.1126/sciadv.ads8318
2025 Harnessing protein language model for structure-based discovery of highly efficient and robust PET hydrolases. Nat Commun doi:10.1038/s41467-025-61599-z
2025 Machine Learning-Guided Identification of PET Hydrolases from Natural Diversity. Acs Catalysis doi:10.1021/acscatal.5c03460
2025 Computational loop reconstruction based design of efficient PET hydrolases. Commun Biol doi:10.1038/s42003-025-08364-6
2024 Enhancing PET Degrading Enzymes: A Combinatory Approach. Chembiochem doi:10.1002/cbic.202400084
2024 Structural dynamics of the Ca 2+ -regulated cutinase towards structure-based improvement of PET degradation activity. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2024.136597
2024 Streamlined screening of extracellularly expressed PETase libraries for improved polyethylene terephthalate degradation. Biotechnol J doi:10.1002/biot.202400021
2024 Understanding the Catalytic Efficiency of Two Polyester Degrading Enzymes: An Experimental and Theoretical Investigation. Acs Omega doi:10.1021/acsomega.4c06528
2024 The metagenome-derived esterase PET40 is highly promiscuous and hydrolyses polyethylene terephthalate (PET). Febs J. doi:10.1111/febs.16924
2024 Exploring the pH dependence of an improved PETase. Biophys.J. doi:10.1016/j.bpj.2024.04.026
2024 The unique salt bridge network in GlacPETase: a key to its stability. Appl.Environ.Microbiol. doi:10.1128/aem.02242-23
2024 beta-sheet Engineering of IsPETase for PET Depolymerization Engineering (Beijing) doi:10.1016/j.eng.2024.10.015
2023 Concentration-Dependent Inhibition of Mesophilic PETases on Poly(ethylene terephthalate) Can Be Eliminated by Enzyme Engineering. ChemSusChem doi:10.1002/cssc.202202277
2023 Ancestral Sequence Reconstruction Identifies Structural Changes Underlying the Evolution of Ideonella sakaiensis PETase and Variants with Improved Stability and Activity. Biochemistry doi:10.1021/acs.biochem.2c00323
2023 Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties. Nat Commun doi:10.1038/s41467-023-40233-w
2023 Complete decomposition of poly(ethylene terephthalate) by crude PET hydrolytic enzyme produced in Pichia pastoris Chem Eng J doi:10.1016/j.cej.2023.148418
2023 Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange. Protein Sci. doi:10.1002/pro.4757
2023 Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product. Nat Commun doi:10.1038/s41467-023-37415-x
2023 Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases. Nat Commun doi:10.1038/s41467-023-37374-3
2023 Remodeling the polymer-binding cavity to improve the efficacy of PBAT-degrading enzyme. J Hazard Mater doi:10.1016/j.jhazmat.2023.132965
2023 Functional tailoring of a PET hydrolytic enzyme expressed in Pichia pastoris. Bioresour Bioprocess doi:10.1186/s40643-023-00648-1
2023 Improvement of thermostability and activity of PET-degrading enzyme Cut190 towards a detailed understanding and application of the enzymatic reaction mechanism. Biorxiv doi:10.1101/2023.02.26.529345
2022 Low Carbon Footprint Recycling of Post-Consumer PET Plastic with a Metagenomic Polyester Hydrolase. ChemSusChem doi:10.1002/cssc.202101062
2022 Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase. Acs Catalysis doi:10.1021/acscatal.2c02275
2022 Investigation of the halophilic PET hydrolase PET6 from Vibrio gazogenes. Protein Sci. doi:10.1002/pro.4500
2022 Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity Nat Commun doi:10.1038/s41467-022-35237-x
2022 Machine learning-aided engineering of hydrolases for PET depolymerization. Nature doi:10.1038/s41586-022-04599-z
2022 Comparative Performance of PETase as a Function of Reaction Conditions, Substrate Properties, and Product Accumulation. ChemSusChem doi:10.1002/cssc.202101932
2022 Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin. Nat Commun doi:10.1038/s41467-022-34908-z