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5KNU

Crystal structure of E. coli hypoxanthine phosphoribosyltransferase in complexed with 9-[N,N-(Bis-3-phosphonopropyl)aminomethyl]-9-deazahypoxanthine

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
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0043101biological_processpurine-containing compound salvage
A0046100biological_processhypoxanthine metabolic process
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0052657molecular_functionguanine phosphoribosyltransferase activity
A0097216molecular_functionguanosine tetraphosphate binding
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
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0043101biological_processpurine-containing compound salvage
B0046100biological_processhypoxanthine metabolic process
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
B0052657molecular_functionguanine phosphoribosyltransferase activity
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 6WA A 201
ChainResidue
AASP107
AASP163
AHOH301
AHOH302
AHOH306
AHOH330
ASER108
AGLY109
ATHR111
ALYS135
AGLU155
APHE156
AVAL157
AILE162

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 202
ChainResidue
AGLU103
AASP104
AHOH322
AHOH326
AHOH327
AHOH332

site_idAC3
Number of Residues4
Detailsbinding site for residue EPE A 203
ChainResidue
AVAL11
APRO14
AGLU15
ATYR173

site_idAC4
Number of Residues16
Detailsbinding site for residue 6WA B 201
ChainResidue
BSER73
BILE105
BILE106
BASP107
BSER108
BGLY109
BLEU112
BLYS135
BARG138
BVAL157
BILE162
BASP163
BHOH301
BHOH305
BHOH311
BHOH321

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 202
ChainResidue
BGLU103
BASP104
BHOH325
BHOH327
BHOH331

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDSGnT
ChainResidueDetails
AVAL99-THR111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12070315","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P9WHQ9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12070315","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GRV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12070315","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G9S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12070315","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G9T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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