› 3oyo

X-ray diffraction
2.1Å resolution

Crystal structure of hemopexin fold protein CP4 from cow pea

Released:
DOI: 10.2210/pdb3oyo/pdb
PDB 3oyo coloured by chain and viewed from the front.
PDB 3oyo coloured by chain and viewed from the side.
PDB 3oyo coloured by chain and viewed from the top.
Source organism: Vigna unguiculata
Primary publication:
The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants.
Gaur V, Chanana V, Jain A, Salunke DM
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 193-200 (2011)
PMID: 21301085

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemopexin fold protein CP4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 24.74 KDa
Source organism: Vigna unguiculata
UniProt:
  • Canonical: F2Z290 (Residues: 1-225; Coverage: 100%)
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand CL 2 x CL
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 125.087Å b: 60.138Å c: 67.574Å
α: 90° β: 111.18° γ: 90°
R-values:
R R work R free
0.209 0.205 0.246

Quick links

Citations

5 citation in other articles

A structurally novel hemopexin fold protein of rice plays role in chlorophyll degradation.
Chattopadhyay et al. (2012)
4 more

2 mentions without citation

The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants.
Gaur et al. (2011)
1 more