› 2x15

X-ray diffraction
2.1Å resolution

The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 1,3- bisphosphoglycerate

Released:
DOI: 10.2210/pdb2x15/pdb
PDB entry 2x15 coloured by chain, front view.
PDB entry 2x15 coloured by chain, side view.
PDB entry 2x15 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Bowler MW, Cliff MJ, Marston JPM, Baxter NJ, Hounslow AMH, Varga AV, Szabo J, Vas M, Blackburn GM, Waltho JP

Function and Biology Details

Reaction catalysed: 
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132717 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 44.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00558 (Residues: 2-417; Coverage: 100%)
Gene names: MIG10, OK/SW-cl.110, PGK1, PGKA
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

5 bound ligands:
Ligand MG 1 x MG
Ligand ADP 1 x ADP
Ligand X15 1 x X15
Ligand 3PG 1 x 3PG
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 38.73Å b: 91.75Å c: 108.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.238
Expression system: Escherichia coli BL21

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