› 3tm9

X-ray diffraction
1.72Å resolution

Y29A mutant of Vitreoscilla stercoraria hemoglobin

Released:
DOI: 10.2210/pdb3tm9/pdb
PDB entry 3tm9 coloured by chain, front view.
PDB entry 3tm9 coloured by chain, side view.
PDB entry 3tm9 coloured by chain, top view.
Source organism: Vitreoscilla stercoraria
Primary publication:
Crystallographic structure determination of B10 mutants of Vitreoscilla hemoglobin: role of Tyr29 (B10) in the structure of the ligand-binding site.
Ratakonda S, Anand A, Dikshit K, Stark BC, Howard AJ
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 215-22 (2013)
PMID: 23519792

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterial hemoglobin Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 15.7 KDa
Source organism: Vitreoscilla stercoraria
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P04252 (Residues: 1-146; Coverage: 100%)
Gene name: vhb
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand EDO 12 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 85.194Å b: 46.426Å c: 62.873Å
α: 90° β: 128.84° γ: 90°
R-values:
R R work R free
0.176 0.172 0.206
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

3 review citations

Recent applications of Vitreoscilla hemoglobin technology in bioproduct synthesis and bioremediation.
Stark et al. (2015)
2 more

1 mention without citation

Crystallographic structure determination of B10 mutants of Vitreoscilla hemoglobin: role of Tyr29 (B10) in the structure of the ligand-binding site.
Ratakonda et al. (2013)