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1G9T

CRYSTAL STRUCTURE OF E.COLI HPRT-GMP COMPLEX

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
A0006178biological_processguanine salvage
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
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
B0006178biological_processguanine salvage
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
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 Residues16
DetailsBINDING SITE FOR RESIDUE 5GP A 190
ChainResidue
AGLU103
APHE156
AVAL157
AILE162
AASP163
AHOH1001
AHOH1011
AHOH1090
AILE105
AASP107
ASER108
AGLY109
AASN110
ATHR111
ALEU112
ALYS135

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
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12070315
ChainResidueDetails
AASP107
BASP407

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WHQ9
ChainResidueDetails
BGLY348
BARG469
AGLY48
AARG169
BARG347
AARG47

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV
ChainResidueDetails
BGLU403
BASP404
AGLU103
AASP104

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S
ChainResidueDetails
BASP407
BLYS435
ALYS135
AASP107

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9T
ChainResidueDetails
AASP163
BASP463

218500

PDB entries from 2024-04-17

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