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8YPY

Crystal strcuture of human phosphoribosyl pyrophosphate synthetase2 (PRPS2) in complex with ligands

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004749molecular_functionribose phosphate diphosphokinase activity
A0009156biological_processribonucleoside monophosphate biosynthetic process
A0009165biological_processnucleotide biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004749molecular_functionribose phosphate diphosphokinase activity
B0009156biological_processribonucleoside monophosphate biosynthetic process
B0009165biological_processnucleotide biosynthetic process
C0000287molecular_functionmagnesium ion binding
C0004749molecular_functionribose phosphate diphosphokinase activity
C0009156biological_processribonucleoside monophosphate biosynthetic process
C0009165biological_processnucleotide biosynthetic process
D0000287molecular_functionmagnesium ion binding
D0004749molecular_functionribose phosphate diphosphokinase activity
D0009156biological_processribonucleoside monophosphate biosynthetic process
D0009165biological_processnucleotide biosynthetic process
E0000287molecular_functionmagnesium ion binding
E0004749molecular_functionribose phosphate diphosphokinase activity
E0009156biological_processribonucleoside monophosphate biosynthetic process
E0009165biological_processnucleotide biosynthetic process
F0000287molecular_functionmagnesium ion binding
F0004749molecular_functionribose phosphate diphosphokinase activity
F0009156biological_processribonucleoside monophosphate biosynthetic process
F0009165biological_processnucleotide biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00114
Number of Residues16
DetailsPRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHAsQIQGFFdiPVD
ChainResidueDetails
AASP131-ASP146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues75
DetailsRegion: {"description":"Binding of phosphoribosylpyrophosphate","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues47
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40295500","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8YPY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues69
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37248548","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7YK1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues46
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2024","submissionDatabase":"PDB data bank","title":"Structure of human PRPS2 long isoform at 3.4 Angstroms resolution.","authors":["Liu J.L.","Lu G.M."]}},{"source":"PDB","id":"8YI9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40295500","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2024","submissionDatabase":"PDB data bank","title":"Structure of human PRPS2 long isoform at 3.4 Angstroms resolution.","authors":["Liu J.L.","Lu G.M."]}},{"source":"PDB","id":"8YI9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8YPY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

260320

PDB entries from 2026-09-30

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