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

1A95

XPRTASE FROM E. COLI COMPLEXED WITH MG:CPRPP AND GUANINE

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
C0000287molecular_functionmagnesium ion binding
C0000310molecular_functionxanthine phosphoribosyltransferase activity
C0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006166biological_processpurine ribonucleoside salvage
C0016020cellular_componentmembrane
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0032263biological_processGMP salvage
C0032264biological_processIMP salvage
C0032265biological_processXMP salvage
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051289biological_processprotein homotetramerization
C0052657molecular_functionguanine phosphoribosyltransferase activity
C0097216molecular_functionguanosine tetraphosphate binding
D0000287molecular_functionmagnesium ion binding
D0000310molecular_functionxanthine phosphoribosyltransferase activity
D0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006166biological_processpurine ribonucleoside salvage
D0016020cellular_componentmembrane
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0032263biological_processGMP salvage
D0032264biological_processIMP salvage
D0032265biological_processXMP salvage
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051289biological_processprotein homotetramerization
D0052657molecular_functionguanine phosphoribosyltransferase activity
D0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 307
ChainResidue
CPCP302
CHOH533
CHOH534

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 308
ChainResidue
BPCP301
BHOH535
BHOH536

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PCP B 301
ChainResidue
BARG69
BASP88
BASP89
BLEU90
BASP92
BTHR93
BGLY94
BGLY95
BTHR96
BGUN304
BMG308
BHOH466
BHOH535
BHOH536
BSER36
BARG37
BGLY38

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PCP C 302
ChainResidue
CARG37
CGLY38
CARG69
CASP88
CASP89
CLEU90
CASP92
CTHR93
CGLY94
CGLY95
CTHR96
CGUN303
CMG307
CHOH421
CHOH453
CHOH463
CHOH487
CHOH533

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GUN C 303
ChainResidue
CASP92
CLYS115
CTRP134
CILE135
CPCP302
CHOH424
CHOH487

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GUN B 304
ChainResidue
BLEU90
BASP92
BLYS115
BTRP134
BILE135
BPCP301
BHOH435

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BO3 D 305
ChainResidue
BASN67
DVAL35
DSER36
DARG37
DGLY38
DASP88
DHOH422

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BO3 A 306
ChainResidue
AVAL35
ASER36
AARG37
AGLY38
AASP88
AHOH471
CASN67

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 Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95
ChainResidueDetails
AARG37
AASP88
BARG37
BASP88
CARG37
CASP88
DARG37
DASP88

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97
ChainResidueDetails
AARG69
ATRP134
BARG69
BTRP134
CARG69
CTRP134
DARG69
DTRP134

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9100006
ChainResidueDetails
AASP89
BASP89
CASP89
DASP89

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96
ChainResidueDetails
AASP92
AILE135
BASP92
BILE135
CASP92
CILE135
DASP92
DILE135

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)

site_idMCSA3
Number of Residues3
DetailsM-CSA 391
ChainResidueDetails
CASP88electrostatic stabiliser
CASP89electrostatic stabiliser
CASP92proton shuttle (general acid/base)

site_idMCSA4
Number of Residues3
DetailsM-CSA 391
ChainResidueDetails
DASP88electrostatic stabiliser
DASP89electrostatic stabiliser
DASP92proton shuttle (general acid/base)

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon