› 3aq5

X-ray diffraction
1.78Å resolution

Crystal structure of truncated hemoglobin from Tetrahymena pyriformis, Fe(II)-O2 form

Released:
DOI: 10.2210/pdb3aq5/pdb
PDB entry 3aq5 coloured by chain, front view.
PDB entry 3aq5 coloured by chain, side view.
PDB entry 3aq5 coloured by chain, top view.
Source organism: Tetrahymena pyriformis
Primary publication:
A hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxification.
Igarashi J, Kobayashi K, Matsuoka A
J Biol Inorg Chem 16 599-609 (2011)
PMID: 21298303

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148147 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Group 1 truncated hemoglobin Chains: A, B
Molecule details ›
Chains: A, B
Length: 121 amino acids
Theoretical weight: 13.71 KDa
Source organism: Tetrahymena pyriformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P17724 (Residues: 1-121; Coverage: 100%)
Sequence domains: Bacterial-like globin
Structure domains: Globins

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P6522
Unit cell:
a: 69.355Å b: 69.355Å c: 353.761Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.187 0.209
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Hemoglobin: a nitric-oxide dioxygenase.
Gardner PR. (2012)
9 other articles

4 mentions without citation

Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand.
Johnson et al. (2014)
3 more