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2BPQ

Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo structure)

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 Residues8
DetailsBINDING SITE FOR RESIDUE BEN A 1369
ChainResidue
ATHR70
AMET71
ALYS72
AASP225
AHOH2140
BTHR35
BASN37
BGOL1376

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEN B 1374
ChainResidue
BMET69
BTHR70
BMET71
BLYS72
BASP225
AASN37

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BEN B 1375
ChainResidue
BGLY80
BTHR353
BALA355
BHOH2018

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1370
ChainResidue
APHE274
AASP275
AGLY278
APHE279
ATRP336

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1376
ChainResidue
ATHR70
APRO199
ABEN1369
AHOH2073
BTHR35
BASP36

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211
ChainResidueDetails
AGLY107
BGLY107

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AGLY110
BASN117
BSER119
BLYS135
BASN138
BARG193
BASP251
BGLU252
AASN117
ASER119
ALYS135
AASN138
AARG193
AASP251
AGLU252
BGLY110

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
ATHR115
AGLY147
BTHR115
BGLY147

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:21969609
ChainResidueDetails
AALA2
BALA2

222036

PDB entries from 2024-07-03

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