Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3HFR

Crystal structure of glutamate racemase from Listeria monocytogenes

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0042802molecular_functionidentical protein binding
A0047661molecular_functionamino-acid racemase activity
A0071555biological_processcell wall organization
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
B0042802molecular_functionidentical protein binding
B0047661molecular_functionamino-acid racemase activity
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 267
ChainResidue
ATHR74
ATHR116
ATHR119
AHOH272

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 268
ChainResidue
ATHR116
ALEU117

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 6JZ A 269
ChainResidue
ATYR81
BASN222

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 6JZ A 270
ChainResidue
AASP246
ALYS156

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 267
ChainResidue
BASN73
BCYS183
BTHR184
BHOH333

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 6JZ B 268
ChainResidue
ATYR220
AHIS221
BASP88
BTYR220
BHIS221

Functional Information from PROSITE/UniProt
site_idPS00923
Number of Residues9
DetailsASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. VIaC.NTATA
ChainResidueDetails
AVAL69-ALA77

site_idPS00924
Number of Residues11
DetailsASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. VIlGCTHYPlL
ChainResidueDetails
AVAL179-LEU189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"O58403","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22634","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22634","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3IST","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1b73
ChainResidueDetails
ASER10
ACYS183
ACYS72
AASP9

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1b73
ChainResidueDetails
BSER10
BCYS183
BCYS72
BASP9

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon