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1NUL

XPRTASE FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000310molecular_functionxanthine phosphoribosyltransferase activity
A0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006166biological_processpurine ribonucleoside salvage
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0032265biological_processXMP salvage
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0052657molecular_functionguanine phosphoribosyltransferase activity
A0097216molecular_functionguanosine tetraphosphate binding
B0000287molecular_functionmagnesium ion binding
B0000310molecular_functionxanthine phosphoribosyltransferase activity
B0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006166biological_processpurine ribonucleoside salvage
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0032265biological_processXMP salvage
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
B0052657molecular_functionguanine phosphoribosyltransferase activity
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
AARG53
BSER36
BARG37
BGLY38
BLYS106
BHOH762
BHOH795

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AHOH735
AHOH777
AHOH866
AHOH960
AARG37
AGLY38

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BASP89
BHOH955
BHOH956
BHOH957
BHOH958
BHOH959

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AASP88
AASP89
AHOH960
AHOH961
AHOH962
AHOH963
AHOH964

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. FIVIDDLVDTGgT
ChainResidueDetails
APHE84-THR96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95
ChainResidueDetails
AARG37
AASP88
BARG37
BASP88

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97
ChainResidueDetails
AARG69
ATRP134
BARG69
BTRP134

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9100006
ChainResidueDetails
AASP89
BASP89

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96
ChainResidueDetails
AASP92
AILE135
BASP92
BILE135

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 391
ChainResidueDetails
AASP88electrostatic stabiliser
AASP89electrostatic stabiliser
AASP92proton shuttle (general acid/base)

site_idMCSA2
Number of Residues3
DetailsM-CSA 391
ChainResidueDetails
BASP88electrostatic stabiliser
BASP89electrostatic stabiliser
BASP92proton shuttle (general acid/base)

218853

PDB entries from 2024-04-24

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