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2X4Z

Crystal Structure of the Human p21-Activated Kinase 4 in Complex with PF-03758309

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 Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1591
ChainResidue
ASER331
AASP440
ALYS442
A7KC1593
AHOH2079
AHOH2141

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1592
ChainResidue
AGLU366
AASP458
APHE459
AGLY460
AHOH2016
AHOH2069
ATHR332
ALYS350
AMET352

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE X4Z A 1593
ChainResidue
AILE327
AGLY328
AGLY330
ATHR332
AGLY333
AVAL335
AALA348
ALYS350
AMET395
AGLU396
APHE397
ALEU398
AGLU399
AGLY401
AASP444
AASP458
AGOL1591
AHOH2142
AHOH2143
AHOH2144

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

239803

PDB entries from 2025-08-06

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