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4DAN

Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in complex with 2-fluoroadenosine

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
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2FA A 301
ChainResidue
AARG87
ASER202
AASP203
AVAL205
BHIS4
BARG43
ASER90
ACYS91
AGLY92
APHE159
AVAL177
AGLU178
AMET179
AGLU180

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2FA B 301
ChainResidue
AHIS4
AARG43
BARG87
BSER90
BCYS91
BGLY92
BPHE159
BVAL177
BGLU178
BMET179
BGLU180
BSER202
BASP203
BVAL205

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AASP203
BASP203

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P50389
ChainResidueDetails
AHIS4
AARG43
BHIS4
BARG43

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P50389
ChainResidueDetails
AGLY20
BSER202
AARG24
AARG87
AGLU178
ASER202
BGLY20
BARG24
BARG87
BGLU178

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AARG216
BARG216

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PDB entries from 2024-07-17

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