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4MAR

Crystal structure of purine nucleoside phosphorylase from Meiothermus ruber DSM 1279 complexed with sulfate.

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
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AGLU230

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AARG97
AHIS149
AVAL150
AHOH697

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AHOH639
AHOH683
AALA13
AGLU14
AARG56
AHOH619

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AGLY20
AARG24
AARG87
AGLY89
ATHR90
AHOH679
CARG43

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
BALA13
BGLU14
BARG56
BHOH443

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BGLY20
BARG24
BARG43
BARG87
BVAL88
BGLY89
BTHR90

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BARG135
BARG136

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 304
ChainResidue
BARG97
BHIS149
BVAL150
BHOH466

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 301
ChainResidue
AARG43
CGLY20
CASP21
CARG24
CARG87
CGLY89
CTHR90
CHOH429
CHOH459

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 302
ChainResidue
CARG135
CARG136

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 303
ChainResidue
CARG97
CHIS149
CVAL150
CHOH483
CHOH495
CHOH498

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 304
ChainResidue
AASN35
CALA13
CGLU14
CARG56
CHOH413
CHOH437

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

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PDB entries from 2024-07-10

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