› 2vpi

X-ray diffraction
2.4Å resolution

Human GMP synthetase - glutaminase domain

Released:
DOI: 10.2210/pdb2vpi/pdb
PDB entry 2vpi coloured by chain, front view.
PDB entry 2vpi coloured by chain, side view.
PDB entry 2vpi coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Welin M, Tresaugues L, Arrowsmith CH, Berglund H, Busam RD, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Herman MD, Johansson I, Kallas A, Karlberg T, Kotenyova T, Lehtio L, Moche M, Nilsson ME, Nyman T, Persson C, Sagemark J, Svensson L, Thorsell AG, Van Der Berg S, Weigelt J, Nordlund P, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156085 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 23.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49915 (Residues: 11-24, 25-219; Coverage: 30%)
Gene name: GMPS
Sequence domains: Glutamine amidotransferase class-I
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 35.68Å b: 120.88Å c: 47.32Å
α: 90° β: 106.43° γ: 90°
R-values:
R R work R free
0.206 0.203 0.261
Expression system: Escherichia coli BL21(DE3)

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