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3IST

Crystal structure of glutamate racemase from Listeria monocytogenes in complex with succinic acid

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
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
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SIN A 267
ChainResidue
ASER10
ACYS183
AHOH283
AHOH358
AHOH374
ACYS39
APRO40
ATYR41
AGLY42
ATHR74
ATHR116
ATHR119
AVAL147

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SIN B 267
ChainResidue
BSER10
BPRO40
BTYR41
BGLY42
BCYS72
BASN73
BTHR74
BHOH270
BHOH358
BHOH445
BHOH446

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 268
ChainResidue
AHOH273
BARG84
BILE92
BGLY93
BHOH278
BHOH408

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 268
ChainResidue
AGLY42
ATHR116
ALEU117
AHOH374
AHOH520

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
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-Rule:MF_00258
ChainResidueDetails
ACYS72
ACYS183
BCYS72
BCYS183

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-Rule:MF_00258
ChainResidueDetails
AASP9
AASN73
ATHR184
BASP9
BASN73
BTHR184

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-Rule:MF_00258, ECO:0007744|PDB:3IST
ChainResidueDetails
ATYR41
BTYR41

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

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PDB entries from 2024-05-01

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