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3SCZ

Combining crystallographic, thermodynamic, and molecular dynamics studies of Mycobacterium tuberculosis purine nucleoside phosphorylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0006154biological_processadenosine catabolic process
A0006161biological_processdeoxyguanosine catabolic process
A0009116biological_processnucleoside metabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005737cellular_componentcytoplasm
B0006139biological_processnucleobase-containing compound metabolic process
B0006154biological_processadenosine catabolic process
B0006161biological_processdeoxyguanosine catabolic process
B0009116biological_processnucleoside metabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HPA A 269
ChainResidue
AALA121
AHOH363
AGLY122
AGLU189
AGLY206
AMET207
ATHR230
AASN231
ALEU241
AHOH309

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HPA B 269
ChainResidue
BALA120
BALA121
BGLY122
BGLU189
BVAL205
BGLY206
BMET207
BTHR230
BASN231
BHOH316
BHOH340

Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues42
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. LvlaGriHaYeghdLryvVhpVrAaraaGaqi.MVltNAaGGL
ChainResidueDetails
ALEU83-LEU124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11444966, ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80
ChainResidueDetails
ASER36
AARG88
ASER208
BSER36
BARG88
BSER208

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P45563
ChainResidueDetails
AHIS68
AALA120
BHIS68
BALA120

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11444966
ChainResidueDetails
AGLU189
AASN231
BGLU189
BASN231

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PDB entries from 2024-11-13

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