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1PK9

Crystal Structure of E. coli purine nucleoside phosphorylase complexed with 2-fluoroadenosine and sulfate/phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006152biological_processpurine nucleoside catabolic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0042278biological_processpurine nucleoside metabolic process
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006152biological_processpurine nucleoside catabolic process
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0042278biological_processpurine nucleoside metabolic process
C0003824molecular_functioncatalytic activity
C0004731molecular_functionpurine-nucleoside phosphorylase activity
C0005829cellular_componentcytosol
C0006139biological_processnucleobase-containing compound metabolic process
C0006152biological_processpurine nucleoside catabolic process
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0042278biological_processpurine nucleoside metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 309
ChainResidue
AGLY20
AARG43
AARG87
AGLY89
ASER90
A2FA306
AHOH328

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 310
ChainResidue
BGLY89
BSER90
B2FA307
BHOH339
CARG43
BGLY20
BARG87

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 C 311
ChainResidue
BARG43
CGLY20
CARG24
CARG87
CGLY89
CSER90
C2FA308

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2FA A 306
ChainResidue
AHIS4
AARG43
AMET64
AARG87
ASER90
ACYS91
AGLY92
APHE159
AVAL178
AGLU179
AMET180
AGLU181
AASP204
APO4309
AHOH356

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 2FA B 307
ChainResidue
BARG87
BSER90
BCYS91
BGLY92
BPHE159
BVAL178
BGLU179
BMET180
BGLU181
BSER203
BASP204
BPO4310
BHOH402
CHIS4
CARG43
CHOH346

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 2FA C 308
ChainResidue
BHIS4
BARG43
BHOH341
CMET64
CARG87
CSER90
CCYS91
CGLY92
CPHE159
CVAL178
CGLU179
CMET180
CGLU181
CASP204
CPO4311
CHOH326

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL
ChainResidueDetails
AGLY61-LEU76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AASP204
BASP204
CASP204

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12937174
ChainResidueDetails
AHIS4
AARG43
BHIS4
BARG43
CHIS4
CARG43

site_idSWS_FT_FI3
Number of Residues15
DetailsBINDING: in other chain => ECO:0000269|PubMed:12937174
ChainResidueDetails
AGLY20
BSER203
CGLY20
CARG24
CARG87
CGLU179
CSER203
AARG24
AARG87
AGLU179
ASER203
BGLY20
BARG24
BARG87
BGLU179

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AARG217
BARG217
CARG217

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
ALYS26
BLYS26
CLYS26

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a69
ChainResidueDetails
AASP204
AARG217

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a69
ChainResidueDetails
BASP204
BARG217

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a69
ChainResidueDetails
CASP204
CARG217

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PDB entries from 2024-05-01

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