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7UJ5

Crystal structure of glutamate racemase from Helicobacter pylori in complex with D-glutamate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008881molecular_functionglutamate racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0047661molecular_functionamino-acid racemase activity
B0008881molecular_functionglutamate racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0047661molecular_functionamino-acid racemase activity
C0008881molecular_functionglutamate racemase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
C0047661molecular_functionamino-acid racemase activity
D0008881molecular_functionglutamate racemase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
D0047661molecular_functionamino-acid racemase activity
Functional Information from PROSITE/UniProt
site_idPS00923
Number of Residues9
DetailsASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. IVaC.NTASA
ChainResidueDetails
AILE67-ALA75

site_idPS00924
Number of Residues11
DetailsASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. VIlGCTHFPlI
ChainResidueDetails
AVAL177-ILE187

251801

PDB entries from 2026-04-08

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