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4IJ1

Bianthranilate-like analogue bound to anthranilate phosphoribosyltransferase (AnPRT; trpD) in absence of substrates.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0000287molecular_functionmagnesium ion binding
A0004048molecular_functionanthranilate phosphoribosyltransferase activity
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
B0000162biological_processtryptophan biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004048molecular_functionanthranilate phosphoribosyltransferase activity
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 17C A 401
ChainResidue
AMET86
AARG194
AGOL402
AHOH533
AHOH696
AASN138
AALA179
APRO180
AHIS183
ATYR186
AARG187
AALA190
AARG193

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AGLY107
AGLY206
APRO207
A17C401
AHOH697

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 403
ChainResidue
AARG237
ALEU305
AGLY306
AGLY307
AILE351
AGLU357

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD A 404
ChainResidue
ATRP47
AASP50
AGLU342
AARG346

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 17C B 401
ChainResidue
BHIS91
BASN138
BPRO180
BPRO180
BARG181
BHIS183
BTYR186
BARG187
BALA190
BARG194
BGOL403
BHOH536
BHOH679

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BALA46
BTRP47
BASP50
BGLU342
BARG346
BHOH539

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
BHIS91
BPRO162
BARG181
BARG194
B17C401

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
BALA236
BARG237
BARG238
BLEU305
BGLY306
BGLY307
BILE351
BASP352
BGLU357
BHOH592
BHOH663

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211
ChainResidueDetails
AVAL106
BVAL106

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AGLY109
BVAL116
BLEU118
BVAL134
BGLY137
BVAL192
BLEU250
BASP251
AVAL116
ALEU118
AVAL134
AGLY137
AVAL192
ALEU250
AASP251
BGLY109

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211, ECO:0000269|PubMed:16337227, ECO:0000269|PubMed:23363292, ECO:0000269|Ref.4, ECO:0000269|Ref.5
ChainResidueDetails
AASN114
AGLY146
BASN114
BGLY146

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:21969609
ChainResidueDetails
AVAL1
BVAL1

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PDB entries from 2024-07-24

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