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Structure of human serum albumin in complex with myristic acid

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

PDB
7OV1
Type
protein
Length
1,164 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serum albumin
UniProt
P02768
Ligands
MYR
Pockets
17 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSerum albuminprotein58274% helix, 0% strandP02768

Ligands and binding sites

  • MYR · Myristic acid · ligand · 16 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

17 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111020.890.90111MYR, EDO
26720.870.9170MYR, EDO
33130.820.9236MYR
43170.820.9236MYR
53870.800.8944MYR

Interfaces

1 interface between chains.

  • A–B · 833 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 34 disulfide (disulfide).

Compared structures

  • P02768 · AlphaFold monomer V2.0 prediction for albumin (P02768) · a predicted model of the same protein · chain A against A, TM-score 0.85

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