› 4o3f

X-ray diffraction
2.11Å resolution

Crystal Structure of mouse PGK1 3PG and terazosin(TZN) ternary complex

Released:
DOI: 10.2210/pdb4o3f/pdb
PDB entry 4o3f coloured by chain, front view.
PDB entry 4o3f coloured by chain, side view.
PDB entry 4o3f coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Terazosin activates Pgk1 and Hsp90 to promote stress resistance.
Chen X, Zhao C, Li X, Wang T, Li Y, Cao C, Ding Y, Dong M, Finci L, Wang JH, Li X, Liu L
Nat Chem Biol 11 19-25 (2015)
PMID: 25383758

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-140647 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 417 amino acids
Theoretical weight: 44.61 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P09411 (Residues: 1-417; Coverage: 100%)
Gene names: Pgk-1, Pgk1
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

2 bound ligands:
Ligand TZN 1 x TZN
Ligand 3PG 1 x 3PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21212
Unit cell:
a: 59.152Å b: 71.397Å c: 92.256Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.213
Expression system: Escherichia coli

Quick links

Citations

12 review citations

PGK1-mediated cancer progression and drug resistance.
He et al. (2019)
11 more

4 mentions without citation

Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.
Rojas-Pirela et al. (2020)
3 more