› 1anw

X-ray diffraction
2.4Å resolution

THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING

Released:
DOI: 10.2210/pdb1anw/pdb
PDB entry 1anw coloured by chain, front view.
PDB entry 1anw coloured by chain, side view.
PDB entry 1anw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The effect of metal binding on the structure of annexin V and implications for membrane binding.
Lewit-Bentley A, Morera S, Huber R, Bodo G
Eur J Biochem 210 73-7 (1992)
PMID: 1446685

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140372 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Annexin A5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 319 amino acids
Theoretical weight: 35.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08758 (Residues: 2-320; Coverage: 100%)
Gene names: ANX5, ANXA5, ENX2, PP4
Sequence domains: Annexin
Structure domains: Annexin

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 83.9Å b: 80.9Å c: 71.4Å
α: 90° β: 108.7° γ: 90°
R-values:
R R work R free
0.181 not available not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Annexins: from structure to function.
Gerke et al. (2002)
5 more

2 mentions without citation

NHS-Esters As Versatile Reactivity-Based Probes for Mapping Proteome-Wide Ligandable Hotspots.
Ward et al. (2017)
1 more