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2J0I

CRYSTAL STRUCTURE OF THE HUMAN P21-ACTIVATED KINASE 4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1590
ChainResidue
AASN323
AILE325
AILE337
AALA338
ATHR339
APHE364
AHOH2054

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1591
ChainResidue
ALEU398
AHOH2203
AHOH2204
AILE327
APHE397

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1592
ChainResidue
ALYS350
AASP440
AASP458
AGLY460

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1593
ChainResidue
AGLU366
AVAL379
ALEU456
ASER457
APHE459

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSTGIVCiAtvrssgklv.........AVKK
ChainResidueDetails
AILE327-LYS351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26607847","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4XBR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XBU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26607847","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4XBR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XBU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of the human p21-activated kinase 4.","authors":["Eswaran J.","Debreczeni J.E.","Bunkoczi G.","Filippakopoulos P.","Das S.","Fedorov O.","Sundstrom M.","Arrowsmith C.","Edwards A.","von Delft F.","Knapp S."]}},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP440
AASP444

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP440
ALYS442

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR478
AASP440
ALYS442

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ASER445
AASP440
ALYS442

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PDB entries from 2025-08-06

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