Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5KNR

E. coli HPRT in complexed with 9-[(N-phosphonoethyl-N-phosphonoethoxyethyl)-2-aminoethyl]-guanine

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
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
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 Residues20
Detailsbinding site for residue 3L5 A 201
ChainResidue
AARG47
ATHR111
ALEU112
ALYS135
AARG138
AGLU155
APHE156
AVAL157
AILE162
AASP163
AMG202
AGLY48
AHOH302
AASP104
AILE105
AILE106
AASP107
ASER108
AGLY109
AASN110

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 202
ChainResidue
AGLU103
AASP104
A3L5201
AHOH302

site_idAC3
Number of Residues17
Detailsbinding site for residue 3L5 B 201
ChainResidue
BGLY48
BGLU103
BASP104
BILE105
BILE106
BASP107
BSER108
BGLY109
BASN110
BTHR111
BLYS135
BPHE156
BVAL157
BILE162
BASP163
BARG169
BHOH302

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
BASP107

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WHQ9
ChainResidueDetails
AARG47
AGLY48
AARG169
BARG47
BGLY48
BARG169

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV
ChainResidueDetails
AGLU103
AASP104
BGLU103
BASP104

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S
ChainResidueDetails
AASP107
ALYS135
BASP107
BLYS135

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9T
ChainResidueDetails
AASP163
BASP163

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon