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3TWP

Crystal structure of M. tuberculosis TrpD in complex with an inhibitor

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
C0000162biological_processtryptophan biosynthetic process
C0000287molecular_functionmagnesium ion binding
C0004048molecular_functionanthranilate phosphoribosyltransferase activity
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0046872molecular_functionmetal ion binding
D0000162biological_processtryptophan biosynthetic process
D0000287molecular_functionmagnesium ion binding
D0004048molecular_functionanthranilate phosphoribosyltransferase activity
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211
ChainResidueDetails
AGLY107
BGLY107
CGLY107
DGLY107

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING:
ChainResidueDetails
AGLY110
BASN117
BSER119
BLYS135
BASN138
BARG193
BASP251
BGLU252
CGLY110
CASN117
CSER119
AASN117
CLYS135
CASN138
CARG193
CASP251
CGLU252
DGLY110
DASN117
DSER119
DLYS135
DASN138
ASER119
DARG193
DASP251
DGLU252
ALYS135
AASN138
AARG193
AASP251
AGLU252
BGLY110

site_idSWS_FT_FI3
Number of Residues8
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
CTHR115
CGLY147
DTHR115
DGLY147

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:21969609
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2

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PDB entries from 2024-07-17

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