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4LDN

Crystal structure of a putative purine nucleoside phosphorylase from Vibrio fischeri ES114 (Target NYSGRC-029521)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0006139biological_processnucleobase-containing compound metabolic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0042278biological_processpurine nucleoside metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 301
ChainResidue
AGLY21
AARG25
AARG44
AARG88
ASER91
AHOH404

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 302
ChainResidue
AHOH537
AHIS210
AHIS212
AHOH478

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AASN117
AARG120
APHE126
ATYR174
ASER188

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
ATYR33
ATYR33
AHIS223
AHIS223
AHOH405
AHOH405

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AHIS96
AALA172
AILE176
AHOH455

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AARG44
AARG44
AMSE46
AMSE46
AHOH482

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
ATHR145
AASN227
AASP231
AHOH503

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGaPSaSIyfhEL
ChainResidueDetails
AGLY62-LEU77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AASP205

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P50389
ChainResidueDetails
AHIS5
AARG44

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P50389
ChainResidueDetails
AGLY21
AARG25
AARG88
AGLU180
ATHR204

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627
ChainResidueDetails
AARG218

222624

PDB entries from 2024-07-17

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