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2JFN

Crystal structure of Escherichia coli glutamate racemase in complex with L- Glutamate and activator UDP-MurNAc-ala

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
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
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU A1287
ChainResidue
AASP28
ACYS204
ATHR205
AHIS206
AHOH2089
ASER29
APHE58
APRO59
ATYR60
AGLY61
ACYS92
AASN93
ATHR94

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE UMA A1286
ChainResidue
ALEU100
AARG104
AVAL112
AGLY113
AVAL114
AVAL115
APRO116
AALA117
ALYS119
APRO120
ASER227
AALA230
AILE231
AARG233
AARG234
AHOH2084
AHOH2166
AHOH2213
AHOH2214
AHOH2215
AHOH2217
AHOH2218
AHOH2220
AHOH2221

Functional Information from PROSITE/UniProt
site_idPS00923
Number of Residues9
DetailsASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. VVaC.NTAST
ChainResidueDetails
AVAL89-THR97

site_idPS00924
Number of Residues11
DetailsASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. VVlGCTHFPlL
ChainResidueDetails
AVAL200-LEU210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-Rule:MF_00258
ChainResidueDetails
ACYS92
ACYS204

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFN
ChainResidueDetails
ATYR60
AASN93
ATHR205
AASP28

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFN
ChainResidueDetails
AARG104
AGLY113

219869

PDB entries from 2024-05-15

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