CODSWALLOP

Mono(2-hydroxyethyl) terephthalate hydrolase

Piscinibacter sakaiensis · seed A0A0K8P8E7 · 603 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.

10Entries 10Entities 6Constructs 1Organisms 5Ligand-bound
1.60 ÅBest res.
2.10 ÅMedian res.

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

The reference structure

6JTU, 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 6JTU
6JTU 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.

130160310 constructs

Constructs, most-used first

6 distinct constructs across 10 entries. 10 polymer entities differ from the UniProt canonical sequence in some way, 4 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
3 596 2.05 6QG9 residues 8-603; L9N, L10H, A11K +8 more
3 611 1.60 6QZ3 His6
1 564 1.70 6QZ1 residues 40-603
1 592 2.65 8EKG residues 12-603; S12M, V13E, A14N +8 more
1 613 2.10 6JTU 1-residue insertion after 16; M1L, Q2A, T3V +10 more
1 621 2.51 6JTT His6; 1-residue insertion after 16; M1L, Q2A, T3V +10 more

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".

S12V 67% V13H 67% L9N 62% L10H 62% A11K 62% L15H 56% A14H 44% A16H 44% A17H 44% C18H 44% A19M 44% M1L 40% Q2A 40% T3V 40% T4A 40% T6A 40% T7A 40% M8G 25% T159V 10% M192Y 10% Y252F 10% Y503W 10%

What it assembles into

Oligomeric stateChainsEntriesShare
monomeric1 10 100.0%

2 entries have the depositor's assembly corroborated by PISA, 8 carry the depositor's word alone and 0 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run.

What binds it

BEZ BEZ3 entries C9C C9C1 entries C8X C8X1 entries J1K J1K1 entries
ComponentClassNameEntriesBest (Å)
CAion Calcium Ion 10 1.60
SO4ion Sulfate Ion 4 1.80
EDOcryoprotectant 1,2-Ethanediol 3 2.05
BEZligand Benzoic Acid 3 1.60
ACTcryoprotectant Acetate Ion 2 2.05
MPDcryoprotectant (4s)-2-Methyl-2,4-Pentanediol 2 2.10
CLion Chloride Ion 2 2.10
C9Cligand 4-(2-Hydroxyethyloxycarbonyl)benzoic Acid 1 2.51
C8Xligand Bis(2-Hydroxyethyl) Benzene-1,4-Dicarboxylate 1 2.51
GOLcryoprotectant Glycerol 1 2.10
FMTbuffer Formic Acid 1 2.10
ZNion Zinc Ion 1 2.05
J1Kligand 4-(2-Hydroxyethylcarbamoyl)benzoic Acid 1 2.10
PEGcryoprotectant Di(Hydroxyethyl)ether 1 2.65

How it crystallises

Parsed from the free text 10 depositors typed into _exptl_crystal_grow.pdbx_details, out of 10 entries that recorded anything at all. Median pH 6.5 (range 4.5 to 7.3).

Precipitants

PEG × Tacsimate × Ammonium sulfate × MPD × Sodium citrate × Ammonium phosphate × Magnesium chloride ×

Buffers

HEPES × MES × Sodium acetate × Citrate × Sodium cacodylate ×

Which entries to trust

10 entries carry a wwPDB validation report: 10 clean, 0 worth a check and 0 with something to explain. Median clashscore 3.79, median RSRZ outliers 1.25%, median R-free minus R-work 0.027. 10 have released structure factors.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Pseudideonella sakaiensis10 1.60 5 100%

Seed sequence

603 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

1MQTTVTTMLL ASVALAACAG GGSTPLPLPQ QQPPQQEPPP PPVPLASRAA CEALKDGNGD
61MVWPNAATVV EVAAWRDAAP ATASAAALPE HCEVSGAIAK RTGIDGYPYE IKFRLRMPAE
121WNGRFFMEGG SGTNGSLSAA TGSIGGGQIA SALSRNFATI ATDGGHDNAV NDNPDALGTV
181AFGLDPQARL DMGYNSYDQV TQAGKAAVAR FYGRAADKSY FIGCSEGGRE GMMLSQRFPS
241HYDGIVAGAP GYQLPKAGIS GAWTTQSLAP AAVGLDAQGV PLINKSFSDA DLHLLSQAIL
301GTCDALDGLA DGIVDNYRAC QAAFDPATAA NPANGQALQC VGAKTADCLS PVQVTAIKRA
361MAGPVNSAGT PLYNRWAWDA GMSGLSGTTY NQGWRSWWLG SFNSSANNAQ RVSGFSARSW
421LVDFATPPEP MPMTQVAARM MKFDFDIDPL KIWATSGQFT QSSMDWHGAT STDLAAFRDR
481GGKMILYHGM SDAAFSALDT ADYYERLGAA MPGAAGFARL FLVPGMNHCS GGPGTDRFDM
541LTPLVAWVER GEAPDQISAW SGTPGYFGVA ARTRPLCPYP QIARYKGSGD INTEANFACA
601APP

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
2024 Increasing the Soluble Expression and Whole-Cell Activity of the Plastic-Degrading Enzyme MHETase through Consensus Design. Biochemistry doi:10.1021/acs.biochem.4c00165
2020 Characterization and engineering of a two-enzyme system for plastics depolymerization. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2006753117
2020 Decomposition of PET film by MHETase using Exo-PETase function Acs Catalysis doi:10.1021/acscatal.9b05604
2019 Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate. Nat Commun doi:10.1038/s41467-019-09326-3