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Crystal structure of human serum albumin

Analyse Crystal structure of human serum albumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BM0
Type
protein
Length
1,156 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serum albumin
UniProt
P02768
Pockets
17 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSerum albuminprotein57873% helix, 0% strandP02768

Pockets

17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110520.860.87116empty
210430.860.87118empty
3750.680.9421empty
42200.590.8020empty
52130.580.8022empty

Interfaces

1 interface between chains.

  • A–B · 506 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 34 disulfide (disulfide).

Compared structures

  • 1BM0 · Crystal structure of human serum albumin · the same entry in another collection · chain A against A, TM-score 1.00
  • P02768 · AlphaFold monomer V2.0 prediction for albumin (P02768) · a predicted model of the same protein · chain A against A, TM-score 0.98

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