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4IJZ

Crystal structure of diaminopimelate epimerase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008047molecular_functionenzyme activator activity
A0008837molecular_functiondiaminopimelate epimerase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016853molecular_functionisomerase activity
A0042803molecular_functionprotein homodimerization activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008047molecular_functionenzyme activator activity
B0008837molecular_functiondiaminopimelate epimerase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016853molecular_functionisomerase activity
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 301
ChainResidue
AALA132
AASN133
ALYS134
ATYR139
AARG184
AHOH516
BPHE24
BPHE25
BSER26

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 A 302
ChainResidue
AVAL23
AGLU49
AHOH437
BARG142

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 B 301
ChainResidue
APHE24
APHE25
ASER26
BALA132
BASN133
BLYS134
BTYR139
BARG184
BHOH427
BHOH551

Functional Information from PROSITE/UniProt
site_idPS01326
Number of Residues15
DetailsDAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevaqCGNGaR
ChainResidueDetails
AASN64-ARG78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00197
ChainResidueDetails
ACYS73
BCYS73

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00197
ChainResidueDetails
ACYS217
BCYS217

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00197
ChainResidueDetails
BASN64
BGLY74
BASN157
BASN190
BGLU208
BGLY218
AGLY74
AASN157
AASN190
AGLU208
AGLY218
BASN11
BGLN44
AASN11
AGLN44
AASN64

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197
ChainResidueDetails
AHIS159
AGLU208
BHIS159
BGLU208

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for dimerization => ECO:0000269|PubMed:23426375
ChainResidueDetails
ATYR268
BTYR268

219869

PDB entries from 2024-05-15

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