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9N4U

Crystal structure of PAK1 bound to compound R1

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
B0004364molecular_functionglutathione transferase activity
B0006749biological_processglutathione metabolic process
B0016740molecular_functiontransferase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGASGTVYtAmdvatgqe..........VAIK
ChainResidueDetails
AILE276-LYS299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues251
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"22153498","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22153498","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by JAK2","evidences":[{"source":"PubMed","id":"17726028","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17989089","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis, BRSK2 and PDPK1","evidences":[{"source":"PubMed","id":"10551809","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10995762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22153498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22669945","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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