› 1oxy

X-ray diffraction
2.4Å resolution

CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES

Released:
DOI: 10.2210/pdb1oxy/pdb
PDB entry 1oxy coloured by chain, front view.
PDB entry 1oxy coloured by chain, side view.
PDB entry 1oxy coloured by chain, top view.
Source organism: Limulus polyphemus
Primary publication:
Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences.
Magnus KA, Hazes B, Ton-That H, Bonaventura C, Bonaventura J, Hol WG
Proteins 19 302-9 (1994)
PMID: 7984626

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137536 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemocyanin II Chain: A
Molecule details ›
Chain: A
Length: 628 amino acids
Theoretical weight: 72.66 KDa
Source organism: Limulus polyphemus
Expression system: Not provided
UniProt:
  • Canonical: P04253 (Residues: 1-628; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CU 2 x CU
Ligand OXY 1 x OXY
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 117.24Å b: 117.24Å c: 285.86Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Not provided

Quick links

Citations

18 review citations

Direct electron transfer between copper-containing proteins and electrodes.
Shleev et al. (2005)
17 more

10 mentions without citation

Copper active sites in biology.
Solomon et al. (2014)
9 more