› 4l2m

X-ray diffraction
2.25Å resolution

Crystal structure of the 2/2 hemoglobin from Synechococcus sp. PCC 7002 in the cyanomet state and with covalently attached heme

Released:
DOI: 10.2210/pdb4l2m/pdb
Model geometry
Fit model/data
PDB entry 4l2m coloured by chain, front view.
PDB entry 4l2m coloured by chain, side view.
PDB entry 4l2m coloured by chain, top view.
Source organism: Synechococcus sp. PCC 7002
Primary publication:
The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: comparison of X-ray and NMR structures.
Wenke BB, Lecomte JT, Héroux A, Schlessman JL
Proteins 82 528-34 (2014)
PMID: 23999883

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-186041 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Group 1 truncated hemoglobin Chains: A, B
Molecule details ›
Chains: A, B
Length: 123 amino acids
Theoretical weight: 13.74 KDa
Source organism: Synechococcus sp. PCC 7002
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8RT58 (Residues: 2-124; Coverage: 99%)
Gene names: SYNPCC7002_A1621, glbN
Sequence domains: Bacterial-like globin
Structure domains: Globins

Ligands and Environments

3 bound ligands:
Ligand HEB 2 x HEB
Ligand CYN 2 x CYN
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 50.622Å b: 40.951Å c: 66.461Å
α: 90° β: 111.21° γ: 90°
R-values:
R R work R free
0.221 0.218 0.288
Expression system: Escherichia coli BL21(DE3)

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Citations

9 citation in other articles

A novel tyrosine-heme C−O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins.
Yan et al. (2015)
8 more

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