2h5g

X-ray diffraction
2.25Å resolution

Crystal structure of human pyrroline-5-carboxylate synthetase

Released:
Source organism: Homo sapiens
Entry authors: Papagrigoriou E, Shafqat N, Turnbull AP, Berridge G, Hozjan V, Kavanagh K, Gileadi O, Smee C, Bray J, Gorrec F, Sundstrom M, Arrowsmith C, Weigelt J, Edwards A, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reactions catalysed:
L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH
ATP + L-glutamate = ADP + L-glutamate 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-157120 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-1-pyrroline-5-carboxylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 463 amino acids
Theoretical weight: 51.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54886 (Residues: 362-795; Coverage: 55%)
Gene names: ALDH18A1, GSAS, P5CS, PYCS
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21212
Unit cell:
a: 122.022Å b: 137.402Å c: 72.057Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.272
Expression system: Escherichia coli