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2JFY

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0006807biological_processobsolete nitrogen compound metabolic process
A0008360biological_processregulation of cell shape
A0008881molecular_functionglutamate racemase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016853molecular_functionisomerase activity
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0036361molecular_functionracemase activity, acting on amino acids and derivatives
A0042802molecular_functionidentical protein binding
A0071555biological_processcell wall organization
B0006807biological_processobsolete nitrogen compound metabolic process
B0008360biological_processregulation of cell shape
B0008881molecular_functionglutamate racemase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016853molecular_functionisomerase activity
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0036361molecular_functionracemase activity, acting on amino acids and derivatives
B0042802molecular_functionidentical protein binding
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DGL A1256
ChainResidue
AASP7
ACYS181
ATHR182
AHIS183
AHOH2094
AHOH2136
ASER8
APRO38
ATYR39
AGLY40
ACYS70
AASN71
ATHR72
ATHR116

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DGL B1256
ChainResidue
BASP7
BSER8
BPRO38
BTYR39
BGLY40
BCYS70
BASN71
BTHR72
BTHR116
BCYS181
BTHR182
BHIS183
BHOH2098
BHOH2211

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. IIlGCTHFPlI
ChainResidueDetails
AILE177-ILE187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-Rule:MF_00258
ChainResidueDetails
ACYS70
ACYS181
BCYS70
BCYS181

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:19097892, ECO:0000269|PubMed:22877632, ECO:0007744|PDB:2JFX, ECO:0007744|PDB:2JFY, ECO:0007744|PDB:2JFZ, ECO:0007744|PDB:2W4I, ECO:0007744|PDB:4B1F
ChainResidueDetails
AASP7
ATYR39
AASN71
ATHR182
BASP7
BTYR39
BASN71
BTHR182

219869

PDB entries from 2024-05-15

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