CODSWALLOP

Albumin

Homo sapiens · seed P02768 · 609 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.

257Entries 257Entities 45Constructs 10Organisms 172Ligand-bound
1.55 ÅBest res.
2.50 ÅMedian res.

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

The reference structure

1TF0, 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 1TF0
1TF0 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.

1304609255 constructs

Constructs, most-used first

45 distinct constructs across 257 entries. 236 polymer entities differ from the UniProt canonical sequence in some way, 0 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
129 585 1.69 9IK6 residues 25-609
14 583 2.15 5HOZ residues 25-607; R584A
10 609 1.90 8RCO matches the canonical sequence
9 581 2.00 7Y2D residues 27-607
9 583 2.03 9S43 residues 25-607
7 583 2.12 6HN0 residues 25-607
7 585 2.40 2BXK residues 25-609; R545E
6 583 1.92 4ZBQ residues 25-607; L198A, A199G, R394A +1 more
5 583 2.47 4F5S residues 25-607; A214T
5 584 1.89 8BSG residues 25-608; E210K, G211E, S213A
4 582 1.91 9CSG residues 27-608
4 583 1.55 6HN1 matches the canonical sequence
4 584 2.10 7AAI residues 26-609
4 591 2.40 8Y9T residues 19-609
3 585 1.95 6QIO residues 25-609; V442M, T444A, E529G +1 more
3 586 1.90 6FAK TEV site; residues 22-599
2 583 2.50 7EEK residues 26-608
2 585 2.70 1HK5 residues 25-609; R242H
2 607 2.80 6QS9 matches the canonical sequence
2 609 2.60 7YIM matches the canonical sequence
2 610 1.90 9EOD matches the canonical sequence
1 189 residues 226-414
1 192 residues 415-606
1 197 residues 29-225
1 201 residues 409-609

Showing the 25 most-used of 45.

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".

V144P 26% D211E 26% K543D 26% K160G 26% E208A 26% T267K 26% M322L 26% M353T 26% T379A 26% K597P 26% K426D 26% R545K 26% V31I 26% A45G 26% A116E 26% R138K 26% T149A 26% F181H 26% K183E 26% A188D 26% G213I 26% S328A 26% A344K 26% A387E 26% N453T 26% Q483R 26% D495E 26% S541P 26% D573G 26% T590A 26%

What it assembles into

Oligomeric stateChainsEntriesShare
monomeric1 228 88.7%
dimeric2 14 5.4%
trimeric3 8 3.1%
pentameric5 5 1.9%
octameric8 1 0.4%
tetrameric4 1 0.4%

162 entries have the depositor's assembly corroborated by PISA, 78 carry the depositor's word alone and 14 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 4 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 4G03, 4G04, 4K71, 6M5E.

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.

CATHImmunoglobulins1.10.246.10SCOP2BSerum albumin-likeSerum albumin-likeSerum albumin-like1304609
DomainSourceSpan (seed)Chains
ImmunoglobulinsCATH 2.60.40.10 129–234 3
1.10.246.10CATH 229–320 1,016
Serum albumin-likeSCOP2B 8033044 27–220 178
Serum albumin-likeSCOP2B 8033045 221–412 179
Serum albumin-likeSCOP2B 8033047 413–607 178

What binds it

LMR LMR10 entries T44 T448 entries DIF DIF7 entries NPS NPS6 entries OCA OCA6 entries DIU DIU5 entries IMN IMN4 entries SAL SAL4 entries DKA DKA3 entries DAO DAO3 entries RWF RWF3 entries AZQ AZQ3 entries
ComponentClassNameEntriesBest (Å)
MYRlipid/detergent Myristic Acid 61 1.89
ACTcryoprotectant Acetate Ion 23 1.89
PLMlipid/detergent Palmitic Acid 20 2.00
SO4ion Sulfate Ion 19 2.15
MLIbuffer Malonate Ion 16 2.03
FMTbuffer Formic Acid 16 2.03
PO4ion Phosphate Ion 15 2.10
PGEcryoprotectant Triethylene Glycol 15 1.90
SINbuffer Succinic Acid 13 1.92
EDOcryoprotectant 1,2-Ethanediol 12 1.90
PG4cryoprotectant Tetraethylene Glycol 11 1.90
CLion Chloride Ion 10 1.55
LMRligand (2s)-2-Hydroxybutanedioic Acid 10 1.92
T44ligand 3,5,3',5'-Tetraiodo-L-Thyronine 8 1.69
PEGcryoprotectant Di(Hydroxyethyl)ether 8 1.90
UNXion Unknown Atom Or Ion 7 2.25
GOLcryoprotectant Glycerol 7 2.15
DIFligand 2-[2,6-Dichlorophenyl)amino]benzeneacetic Acid 7 1.55
ZNion Zinc Ion 7 2.20
NPSligand (2s)-2-(6-Methoxynaphthalen-2-Yl)propanoic Acid 6 2.19

How it crystallises

Parsed from the free text 188 depositors typed into _exptl_crystal_grow.pdbx_details, out of 237 entries that recorded anything at all. Median pH 7.0 (range 1.0 to 9.0).

Precipitants

PEG × Ammonium sulfate × Sodium chloride × PEG (unspecified) × Tacsimate × Lithium sulfate × MPD × Jeffamine × Isopropanol × Ammonium phosphate × Sodium citrate × Magnesium chloride × Ethanol ×

Buffers

Phosphate × Tris × Citrate × HEPES × MES × Sodium acetate × Sodium cacodylate × Bis-Tris ×

Which entries to trust

254 entries carry a wwPDB validation report: 87 clean, 80 worth a check and 87 with something to explain. Median clashscore 8.42, median RSRZ outliers 1.55%, median R-free minus R-work 0.05. 250 have released structure factors.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Homo sapiens195 1.69 131 100%
Equus caballus31 1.92 20 96%
Bos taurus9 2.47 5 100%
Ovis aries7 2.12 7 96%
Oryctolagus cuniculus6 1.89 4 96%
Capra hircus5 1.55 4 96%
Escherichia coli1 2.00 1 96%
Canis lupus familiaris1 3.20 0 96%
Felis catus1 3.40 0 96%
synthetic construct1 4.00 0 96%

Seed sequence

609 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

1MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF
61EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP
121ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF
181FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV
241ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK
301ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR
361RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE
421QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV
481LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL
541SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV
601AASQAALGL

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 Structural Interactions of beta-Lactam Antibiotics with Mammalian Serum Albumins. Int J Mol Sci doi:10.3390/ijms27020776
2026 Cryo-EM elucidates the interaction mechanism of ozoralizumab, a humanized anti-TNF alpha NANOBODY® compound. Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2026.153572
2025 Structural categorization and identification of electrostatic interactions in two proposed human serum albumin dimerization patterns and dipyridamole interaction. Turk J Chem doi:10.55730/1300-0527.3769
2025 Conversion of albumin into a BODIPY-like photosensitizer by a flick reaction, tumor accumulation and photodynamic therapy. Biomaterials doi:10.1016/j.biomaterials.2024.122792
2025 Insights into Dual Binding Modes of Nateglinide to Human Serum Albumin. Acs Med.Chem.Lett. doi:10.1021/acsmedchemlett.5c00277
2025 Fluorogen-Activating Human Serum Albumin for Mitochondrial Nanoscale Imaging. Adv Mater doi:10.1002/adma.202501849
2025 Albumins constrainting the conformation of mitochondria-targeted photosensitizers for tumor-specific photodynamic therapy. Biomaterials doi:10.1016/j.biomaterials.2024.122914
2025 Cytotoxicity and Binding to DNA, Lysozyme, Ribonuclease A, and Human Serum Albumin of the Diiodido Analog of Picoplatin. Inorg.Chem. doi:10.1021/acs.inorgchem.4c05424
2024 Structural and mechanistic insights into the transport of aristolochic acids and their active metabolites by human serum albumin. J.Biol.Chem. doi:10.1016/j.jbc.2024.107358
2024 Cerastecin Inhibition of the Lipooligosaccharide Transporter MsbA to Combat Acinetobacter baumannii : From Screening Impurity to In Vivo Efficacy. J.Med.Chem. doi:10.1021/acs.jmedchem.4c01277
2024 Structural design of the anti-TNF alpha therapeutic NANOBODY® compound, ozoralizumab, to support its potent and sustained clinical efficacy. Biochem.Biophys.Res.Commun. doi:10.1016/j.bbrc.2024.150454
2024 Developing a Copper(II) Isopropyl 2-Pyridyl Ketone Thiosemicarbazone Compound Based on the IB Subdomain of Human Serum Albumin-Indomethacin Complex: Inhibiting Tumor Growth by Remodeling the Tumor Microenvironment. J.Med.Chem. doi:10.1021/acs.jmedchem.3c02378
2024 Insight into the anti-proliferation activity and photoinduced NO release of four nitrosylruthenium isomeric complexes and their HSA complex adducts. Metallomics doi:10.1093/mtomcs/mfae005
2024 Interaction of Cephalosporins with Human Serum Albumin: A Structural Study. J.Med.Chem. doi:10.1021/acs.jmedchem.4c00983
2024 Crystal structure of human serum albumin in complex with megabody reveals unique human and murine cross-reactive binding site. Protein Sci. doi:10.1002/pro.4887
2024 Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites. Commun Biol doi:10.1038/s42003-024-06219-0
2024 The CryoEM structure of human serum albumin in complex with ligands. J.Struct.Biol. doi:10.1016/j.jsb.2024.108105
2023 Structural Investigation of Diclofenac Binding to Ovine, Caprine, and Leporine Serum Albumins. Int J Mol Sci doi:10.3390/ijms24021534
2023 Stable Mammalian Serum Albumins Designed for Bacterial Expression. J.Mol.Biol. doi:10.1016/j.jmb.2023.168191
2023 Structural and biochemical characterisation of Co2+-binding sites on serum albumins and their interplay with fatty acids Chem Sci doi:10.1039/D3SC01723K
2023 Crystal structures of human serum albumin in complex with lysophosphatidylcholine. Biophys.J. doi:10.1016/j.bpj.2023.09.007
2023 Developing a Multitargeted Anticancer Palladium(II) Agent Based on the His-242 Residue in the IIA Subdomain of Human Serum Albumin. J.Med.Chem. doi:10.1021/acs.jmedchem.3c00248
2023 Uniform thin ice on ultraflat graphene for high-resolution cryo-EM. Nat.Methods doi:10.1038/s41592-022-01693-y
2023 Developing an Anticancer Platinum(II) Compound Based on the Uniqueness of Human Serum Albumin. J.Med.Chem. doi:10.1021/acs.jmedchem.3c00001
2023 Structural Basis of the Change in the Interaction Between Mycophenolic Acid and Subdomain IIA of Human Serum Albumin During Renal Failure. J.Med.Chem. doi:10.1021/acs.jmedchem.2c01790
2022 Developing a Copper(II) Agent Based on His-146 and His-242 Residues of Human Serum Albumin Nanoparticles: Integration To Overcome Cisplatin Resistance and Inhibit the Metastasis of Nonsmall Cell Lung Cancer. J.Med.Chem. doi:10.1021/acs.jmedchem.2c00698
2022 Chlorine Atoms of an Aripiprazole Molecule Control the Geometry and Motion of Aripiprazole and Deschloro-aripiprazole in Subdomain IIIA of Human Serum Albumin. Acs Omega doi:10.1021/acsomega.2c02929
2022 Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil. Int J Mol Sci doi:10.3390/ijms23031769
2022 Investigation of the Interaction between Human Serum Albumin and Branched Short-Chain Perfluoroalkyl Compounds. Chem.Res.Toxicol. doi:10.1021/acs.chemrestox.2c00211
2022 Effects of Myristate on the Induced Circular Dichroism Spectra of Aripiprazole Bound to Human Serum Albumin: A Structural-Chemical Investigation Acs Omega doi:10.1021/acsomega.1c06220
2022 Organism-specific differences in the binding of ketoprofen to serum albumin. Iucrj doi:10.1107/S2052252522006820
2022 Developing a Novel Indium(III) Agent Based on Human Serum Albumin Nanoparticles: Integrating Bioimaging and Therapy. J.Med.Chem. doi:10.1021/acs.jmedchem.1c01790
2022 Crystallographic analysis of interaction between cisplatin and human serum albumin: Effect of fatty acid. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2022.06.181
2021 Unveiling the binding mode of perfluorooctanoic acid to human serum albumin. Protein Sci. doi:10.1002/pro.4036
2021 Developing a Novel Anticancer Gold(III) Agent to Integrate Chemotherapy and Immunotherapy. J.Med.Chem. doi:10.1021/acs.jmedchem.1c00050
2021 Cell-penetrating Alphabody protein scaffolds for intracellular drug targeting. Sci Adv doi:10.1126/sciadv.abe1682
2021 Interaction of Benzbromarone with Subdomains IIIA and IB/IIA on Human Serum Albumin as the Primary and Secondary Binding Regions. Mol Pharm. doi:10.1021/acs.molpharmaceut.0c01004
2020 Triantennary GalNAc Molecular Imaging Probes for Monitoring Hepatocyte Function in a Rat Model of Nonalcoholic Steatohepatitis. Adv Sci doi:10.1002/advs.202002997
2020 Structural investigations of stereoselective profen binding by equine and leporine serum albumins. Chirality doi:10.1002/chir.23162
2020 Identification of Binding Sites on Human Serum Albumin for Somapacitan, a Long-Acting Growth Hormone Derivative. Biochemistry doi:10.1021/acs.biochem.0c00019