› 2hz3

X-ray diffraction
1.9Å resolution

The x-ray crystal structure of ferrous Synechocystis hemoglobin H117A mutant with a covalent linkage

Released:
DOI: 10.2210/pdb2hz3/pdb
PDB entry 2hz3 coloured by chain, front view.
PDB entry 2hz3 coloured by chain, side view.
PDB entry 2hz3 coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.
Hoy JA, Smagghe BJ, Halder P, Hargrove MS
Protein Sci 16 250-60 (2007)
PMID: 17242429

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159913 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Group 1 truncated hemoglobin GlbN Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 13.69 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
UniProt:
  • Canonical: P73925 (Residues: 2-124; Coverage: 99%)
Gene names: glbN, slr2097
Sequence domains: Bacterial-like globin
Structure domains: Globins

Ligands and Environments

3 bound ligands:
Ligand CD 2 x CD
Ligand SO2 2 x SO2
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 43.819Å b: 46.919Å c: 62.089Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.24
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase-1.
Kassa et al. (2016)
8 more

1 mention without citation

Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.
Hoy et al. (2007)