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4M0R

Trianthranilate-like analogue bound to anthranilate phosphoribosyltransferase (AnPRT; TrpD).

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processL-tryptophan biosynthetic process
A0000287molecular_functionmagnesium ion binding
A0004048molecular_functionanthranilate phosphoribosyltransferase activity
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
B0000162biological_processL-tryptophan biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004048molecular_functionanthranilate phosphoribosyltransferase activity
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 644 A 600
ChainResidue
AASN138
AHOH877
AHOH886
AALA179
AHIS183
APRO184
ATYR186
AARG187
AALA190
AARG193
AARG194

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
APHE274
AASP275
APHE279
ATRP336
AHOH764
AHOH883

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A 602
ChainResidue
AARG213
ALEU305
AGLY306
AGLY307
AILE351
AASP352
AGLY354
AHOH723

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 603
ChainResidue
AARG42
AALA170
AGLU171
AVAL172
AGLY173
AHOH753
AHOH892

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 644 B 600
ChainResidue
BTHR108
BASN138
BSER145
BALA179
BHIS183
BTYR186
BARG187
BALA190
BARG193
BARG194
BGLY206
BHOH777

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD B 601
ChainResidue
BALA236
BLEU305
BILE351
BASP352
BGLU357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16337227","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23363292","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2011","submissionDatabase":"PDB data bank","title":"Inhibition of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase by blocking of an active site entrance tunnel.","authors":["Castell A.","Short L.F.","Evans G.","Bulloch E.M.","Cookson T.","Parker E.","Lee C.","Baker E.N.","Lott J.S."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2012","submissionDatabase":"PDB data bank","title":"Improved inhibitors against Mycobacterium tuberculosis anthranilate phosphoribosyltransferase.","authors":["Evans G.L.","Gamage S.A.","Denny W.A.","Baker E.N.","Lott J.S."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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