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4RHY

Crystal structures of Mycobacterium tuberculosis 6-oxopurine phosphoribosyltransferase which is a potential target for drug development against this disease

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006166biological_processpurine ribonucleoside salvage
A0006177biological_processGMP biosynthetic process
A0006178biological_processguanine salvage
A0006188biological_processIMP biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0043101biological_processpurine-containing compound salvage
A0046100biological_processhypoxanthine metabolic process
A0046872molecular_functionmetal ion binding
A0052657molecular_functionguanine phosphoribosyltransferase activity
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006166biological_processpurine ribonucleoside salvage
B0006177biological_processGMP biosynthetic process
B0006178biological_processguanine salvage
B0006188biological_processIMP biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0043101biological_processpurine-containing compound salvage
B0046100biological_processhypoxanthine metabolic process
B0046872molecular_functionmetal ion binding
B0052657molecular_functionguanine phosphoribosyltransferase activity
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006166biological_processpurine ribonucleoside salvage
C0006177biological_processGMP biosynthetic process
C0006178biological_processguanine salvage
C0006188biological_processIMP biosynthetic process
C0016757molecular_functionglycosyltransferase activity
C0032263biological_processGMP salvage
C0032264biological_processIMP salvage
C0043101biological_processpurine-containing compound salvage
C0046100biological_processhypoxanthine metabolic process
C0046872molecular_functionmetal ion binding
C0052657molecular_functionguanine phosphoribosyltransferase activity
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006166biological_processpurine ribonucleoside salvage
D0006177biological_processGMP biosynthetic process
D0006178biological_processguanine salvage
D0006188biological_processIMP biosynthetic process
D0016757molecular_functionglycosyltransferase activity
D0032263biological_processGMP salvage
D0032264biological_processIMP salvage
D0043101biological_processpurine-containing compound salvage
D0046100biological_processhypoxanthine metabolic process
D0046872molecular_functionmetal ion binding
D0052657molecular_functionguanine phosphoribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AGLU122
AASP123
AHOH403
AHOH404
AHOH448
AHOH455

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AHOH402
AHOH405
AHOH447
AASP182
A3QG303
AHOH401

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 3QG A 303
ChainResidue
ALEU65
ALYS66
AGLY67
ASER92
AVAL125
AASP126
ASER127
AGLY128
ALEU129
ATHR130
ALYS154
APHE175
AVAL176
ALEU181
AASP182
AARG188
AMG302
AHOH402
AHOH403
AHOH404
AHOH406
AHOH408
AHOH449
AHOH450
AHOH451

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BGLU122
BASP123
BHOH402
BHOH403
BHOH450
BHOH455

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 302
ChainResidue
BASP182
B3QG303
BHOH401
BHOH404
BHOH405

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 3QG B 303
ChainResidue
BLEU65
BLYS66
BGLY67
BVAL125
BASP126
BSER127
BGLY128
BLEU129
BTHR130
BLYS154
BPHE175
BVAL176
BASP182
BARG188
BMG302
BHOH401
BHOH404
BHOH431
BHOH446
BHOH455

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 301
ChainResidue
CGLU122
CASP123
CHOH401
CHOH402
CHOH403
CHOH446

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 302
ChainResidue
CASP182
C3QG303
CHOH404
CHOH405
CHOH408
CHOH445

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 3QG C 303
ChainResidue
CHOH409
CLEU65
CLYS66
CGLY67
CSER92
CVAL125
CASP126
CSER127
CGLY128
CLEU129
CTHR130
CLYS154
CPHE175
CVAL176
CASP182
CARG188
CMG302
CHOH403
CHOH406
CHOH408

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 301
ChainResidue
DGLU122
DASP123
DHOH401
DHOH402
DHOH403
DHOH407

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 302
ChainResidue
DASP182
D3QG303
DHOH406
DHOH413
DHOH453
DHOH460

site_idBC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 3QG D 303
ChainResidue
DLYS66
DGLY67
DSER92
DVAL124
DASP126
DSER127
DGLY128
DLEU129
DTHR130
DLYS154
DASP174
DPHE175
DVAL176
DASP182
DARG188
DMG302
DHOH404
DHOH405
DHOH406
DHOH412
DHOH435
DHOH455

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDVVDSGlT
ChainResidueDetails
AVAL118-THR130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P0A9M2
ChainResidueDetails
AASP126
BASP126
CASP126
DASP126

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:25915781, ECO:0007744|PDB:4RHT, ECO:0007744|PDB:5KNP
ChainResidueDetails
ALYS66
DLYS66
DGLY67
DARG188
AGLY67
AARG188
BLYS66
BGLY67
BARG188
CLYS66
CGLY67
CARG188

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:25915781, ECO:0007744|PDB:4RHT
ChainResidueDetails
AGLU122
BASP182
CGLU122
CASP123
CLYS154
CPHE175
CASP182
DGLU122
DASP123
DLYS154
DPHE175
AASP123
DASP182
ALYS154
APHE175
AASP182
BGLU122
BASP123
BLYS154
BPHE175

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PDB entries from 2024-07-24

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