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7ZSN

human purine nucleoside phosphorylase in complex with JS-379

Functional Information from GO Data
ChainGOidnamespacecontents
A0000255biological_processallantoin metabolic process
A0001882molecular_functionnucleoside binding
A0002060molecular_functionpurine nucleobase binding
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006148biological_processinosine catabolic process
A0006149biological_processdeoxyinosine catabolic process
A0006157biological_processdeoxyadenosine catabolic process
A0006166biological_processpurine ribonucleoside salvage
A0006204biological_processIMP catabolic process
A0006738biological_processnicotinamide riboside catabolic process
A0006955biological_processimmune response
A0009116biological_processnucleoside metabolic process
A0009165biological_processnucleotide biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0032743biological_processpositive regulation of interleukin-2 production
A0034418biological_processurate biosynthetic process
A0034774cellular_componentsecretory granule lumen
A0042102biological_processpositive regulation of T cell proliferation
A0042301molecular_functionphosphate ion binding
A0042802molecular_functionidentical protein binding
A0043101biological_processpurine-containing compound salvage
A0046059biological_processdAMP catabolic process
A0046638biological_processpositive regulation of alpha-beta T cell differentiation
A0047975molecular_functionguanosine phosphorylase activity
A0070062cellular_componentextracellular exosome
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues42
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypLwkvTfpVrVfhllGvdt.LVvtNAaGGL
ChainResidueDetails
AVAL79-LEU120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
ChainResidueDetails
ASER33

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P55859
ChainResidueDetails
AHIS64

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
ChainResidueDetails
AARG84

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8
ChainResidueDetails
ATYR88

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA
ChainResidueDetails
AALA116
AGLU201
ASER220
AASN243

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT
ChainResidueDetails
AMET219
AHIS257

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000269|PubMed:9305964
ChainResidueDetails
AASN243

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER251

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 17
ChainResidueDetails
ASER33hydrogen bond donor
AHIS64electrostatic stabiliser
AHIS86electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATYR88electrostatic stabiliser, hydrogen bond donor
AGLU89activator, electrostatic stabiliser, hydrogen bond acceptor
AALA116electrostatic stabiliser, hydrogen bond donor
AMET219electrostatic stabiliser, hydrogen bond donor
ASER220electrostatic stabiliser, hydrogen bond donor
AASN243electrostatic stabiliser, hydrogen bond donor, polar interaction
AHIS257electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-06-12

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