› 4max

X-ray diffraction
1.44Å resolution

Crystal structure of Synechococcus sp. PCC 7002 globin at cryogenic temperature with heme modification

Released:
DOI: 10.2210/pdb4max/pdb
PDB entry 4max coloured by chain, front view.
PDB entry 4max coloured by chain, side view.
PDB entry 4max 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, C
Molecule details ›
Chains: A, B, C
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

2 bound ligands:
Ligand HEB 3 x HEB
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P41212
Unit cell:
a: 68.791Å b: 68.791Å c: 156.059Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.194
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 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)
7 more

8 mentions without citation

Triboelectric nanogenerator sensors for soft robotics aiming at digital twin applications.
Jin et al. (2020)
7 more