› 5zs7

X-ray diffraction
2.68Å resolution

Acetylation of lysine 100 in Phosphoglycerate mutase 1

Released:
DOI: 10.2210/pdb5zs7/pdb
PDB entry 5zs7 coloured by chain, front view.
PDB entry 5zs7 coloured by chain, side view.
PDB entry 5zs7 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Jiang LL, Zhou L

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148422 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphoglycerate mutase 1 Chain: B
Molecule details ›
Chain: B
Length: 233 amino acids
Theoretical weight: 26.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18669 (Residues: 3-235; Coverage: 92%)
Gene names: CDABP0006, PGAM1, PGAMA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
Phosphoglycerate mutase 1 Chain: C
Molecule details ›
Chain: C
Length: 234 amino acids
Theoretical weight: 26.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18669 (Residues: 2-235; Coverage: 92%)
Gene names: CDABP0006, PGAM1, PGAMA
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

2 bound ligands:
Ligand MES 1 x MES
Ligand CL 1 x CL
2 modified residues:
Ligand NEP 1 x NEP
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 78.833Å b: 82.827Å c: 100.232Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.255
Expression system: Escherichia coli

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