› 2auo

X-ray diffraction
1.53Å resolution

Residue F4 plays a key role in modulating the oxygen affinity and cooperatrivity in Scapharca dimeric hemoglobin

Released:
DOI: 10.2210/pdb2auo/pdb
PDB entry 2auo coloured by chain, front view.
PDB entry 2auo coloured by chain, side view.
PDB entry 2auo coloured by chain, top view.
Source organism: Anadara inaequivalvis
Primary publication:
Residue F4 plays a key role in modulating oxygen affinity and cooperativity in Scapharca dimeric hemoglobin.
Knapp JE, Bonham MA, Gibson QH, Nichols JC, Royer WE
Biochemistry 44 14419-30 (2005)
PMID: 16262242

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135420 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Globin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 15.98 KDa
Source organism: Anadara inaequivalvis
Expression system: Escherichia coli
UniProt:
  • Canonical: P02213 (Residues: 1-146; Coverage: 100%)
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand HEM 2 x HEM
Ligand CMO 2 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 93.28Å b: 44Å c: 83.61Å
α: 90° β: 121.98° γ: 90°
R-values:
R R work R free
0.202 0.196 0.216
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Simulations of allosteric transitions.
Elber R. (2011)
3 more

3 mentions without citation

Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering.
Yang et al. (2018)
2 more