8x2s

X-ray diffraction
1.9Å resolution

The Crystal Structure of BPGM from Biortus

Released:
Source organism: Homo sapiens
Entry authors: Wang F, Cheng W, Yuan Z, Qi J, Li J

Function and Biology Details

Reactions catalysed:
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N(tau)-phospho-L-histidine + 2/3-phospho-D-glycerate
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-139735 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bisphosphoglycerate mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 30.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07738 (Residues: 1-259; Coverage: 100%)
Gene name: BPGM
Sequence domains: Histidine phosphatase superfamily (branch 1)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 38.661Å b: 61.524Å c: 122.802Å
α: 90° β: 95.32° γ: 90°
R-values:
R R work R free
0.189 0.187 0.229
Expression system: Escherichia coli