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4X5A

Anthranilate phosphoribosyltransferase variant R193A from Mycobacterium tuberculosis remains ligand-free when co-crystallised with PRPP and Mg

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 Residues7
Detailsbinding site for residue GOL A 401
ChainResidue
AARG237
AARG238
ALEU305
AGLY306
AILE351
AASP352
AGLU357

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
AALA355
AARG362
AHOH503
AHOH505
AHOH513
AARG42
AALA128

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL B 401
ChainResidue
BASP159
BPRO180
BARG181

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL B 402
ChainResidue
BTHR273
BPHE274
BASP275
BTRP336

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL B 403
ChainResidue
BALA236
BARG237
BARG238
BLEU305
BGLY306
BGLY307
BILE351
BASP352
BGLU357

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
BALA193
BASP251
BGLU252
AASN117
ASER119
ALYS135
AASN138
AALA193
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

226707

PDB entries from 2024-10-30

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