› 8rgk

X-ray diffraction
1.9Å resolution

Structure of Human Serum Albumin in complex with Aristolochic Acid at 1.9 A resolution

Released:
DOI: 10.2210/pdb8rgk/pdb
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PDB entry 8rgk coloured by chain, front view.
PDB entry 8rgk coloured by chain, side view.
PDB entry 8rgk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and Mechanistic Insights into the Transport of Aristolochic Acids and their Active Metabolites by Human Serum Albumin.
Pomyalov S, Minetti CA, Remeta DP, Bonala R, Johnson F, Zaitseva I, Iden C, Golebiewska U, Breslauer KJ, Shoham G, Sidorenko VS, Grollman AP
J Biol Chem 107358 (2024)
PMID: 38782206

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Albumin Chains: A, B
Molecule details ›
Chains: A, B
Length: 609 amino acids
Theoretical weight: 69.47 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02768 (Residues: 1-609; Coverage: 100%)
Gene names: ALB, GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341
Sequence domains: Serum albumin family

Ligands and Environments

3 bound ligands:
Ligand MYR 13 x MYR
Ligand EDO 9 x EDO
Ligand GOQ 1 x GOQ
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 94.397Å b: 37.872Å c: 180.248Å
α: 90° β: 105.124° γ: 90°
R-values:
R R work R free
0.243 0.24 0.289

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Citations

1 citations in other articles

A Multi-Spectroscopic and Molecular Docking Analysis of the Biophysical Interaction between Food Polyphenols, Urolithins, and Human Serum Albumin.
Zelenović et al. (2024)

1 mention without citation

Structural and mechanistic insights into the transport of aristolochic acids and their active metabolites by human serum albumin.
Pomyalov et al. (2024)

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