Structure analysis

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

X-ray diffraction
1.74Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 16927.42 Å2
Buried surface area: 1412.36 Å2
Dissociation area: 93.04 Å2
Dissociation energy (ΔGdiss): 11.79 kcal/mol
Dissociation entropy (TΔSdiss): -1.45 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132717

Macromolecules

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
Pfam: Phosphoglycerate kinase
InterPro:
CATH: Phosphoglycerate kinase, N-terminal domain

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