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2Q0N

Structure of human p21 activating kinase 4 (PAK4) in complex with a consensus peptide

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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 592
ChainResidue
AARG298
AARG359
AARG360
AGLU361

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 593
ChainResidue
ASEP474
AHOH70
AARG359
ALEU362
AASN365
AARG439

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 594
ChainResidue
AASN413
AGLU414

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
ALYS574
AARG591
BARG-5
BARG-3

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 595
ChainResidue
ALEU475
ALEU521
AARG528
AEDO596

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 596
ChainResidue
AARG528
AEDO595

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 597
ChainResidue
AHOH265
AGLU396
APHE397
ALEU398
AGLY401

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 598
ChainResidue
AHOH273
AHOH275
AGLU399
AGLN587

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 599
ChainResidue
AVAL407
AHIS409
ATHR410

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 Residues25
DetailsRegion: {"description":"GEF-interaction domain (GID)"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
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_FI4
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_FI5
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 2025-12-17

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