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2GVQ

Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0000287molecular_functionmagnesium ion binding
A0004048molecular_functionanthranilate phosphoribosyltransferase activity
A0005829cellular_componentcytosol
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
B0000162biological_processtryptophan biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004048molecular_functionanthranilate phosphoribosyltransferase activity
B0005829cellular_componentcytosol
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0046872molecular_functionmetal ion binding
C0000162biological_processtryptophan biosynthetic process
C0000287molecular_functionmagnesium ion binding
C0004048molecular_functionanthranilate phosphoribosyltransferase activity
C0005829cellular_componentcytosol
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0046872molecular_functionmetal ion binding
D0000162biological_processtryptophan biosynthetic process
D0000287molecular_functionmagnesium ion binding
D0004048molecular_functionanthranilate phosphoribosyltransferase activity
D0005829cellular_componentcytosol
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BE2 A 346
ChainResidue
AASN109
AALA150
AGLN151
AHIS154
AARG164
AGLY177

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BE2 B 401
ChainResidue
BMET157
BARG164
BPHE173
BBE2402
BASN109
BGLN151
BHIS154

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BE2 B 402
ChainResidue
BGLY79
BTHR80
BHIS107
BASN109
BALA150
BGLY177
BPRO178
BBE2401

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BE2 C 501
ChainResidue
CHIS107
CASN109
CGLY177
CBE2502

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BE2 C 502
ChainResidue
CASN109
CHIS154
CMET157
CARG164
CBE2501

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BE2 D 601
ChainResidue
DGLY79
DTHR80
DHIS107
DASN109
DGLY177
DPRO178
DBE2602

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BE2 D 602
ChainResidue
DASN109
DALA150
DGLN151
DHIS154
DMET157
DARG164
DBE2601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING:
ChainResidueDetails
ATHR77
AGLU224
BTHR77
BGLY79
BGLY82
BASN89
BSER91
BLYS106
BASN109
BARG164
BASP223
AGLY79
BGLU224
CTHR77
CGLY79
CGLY82
CASN89
CSER91
CLYS106
CASN109
CARG164
CASP223
AGLY82
CGLU224
DTHR77
DGLY79
DGLY82
DASN89
DSER91
DLYS106
DASN109
DARG164
DASP223
AASN89
DGLU224
ASER91
ALYS106
AASN109
AARG164
AASP223

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211, ECO:0000269|PubMed:16714288, ECO:0000269|PubMed:19385665
ChainResidueDetails
ATHR87
ASER118
BTHR87
BSER118
CTHR87
CSER118
DTHR87
DSER118

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PDB entries from 2024-10-30

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