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4FIF

Catalytic domain of human PAK4 with RPKPLVDP peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP A 1000
ChainResidue
AGLU329
AGLU396
ALEU398
ALEU447
AASP458
APHE459
AGLY460
APHE461
AHOH1118
AHOH1119
AHOH1125
AGLY330
ASER331
ATHR332
AVAL335
AALA348
ALYS350
AGLU366
AMET395

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP B 1000
ChainResidue
BGLU329
BGLY330
BSER331
BTHR332
BVAL335
BALA348
BLYS350
BGLU366
BMET395
BGLU396
BPHE397
BLEU398
BLEU447
BASP458
BPHE459
BGLY460
BPHE461
BHOH1118
BHOH1119
BHOH1130

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR CHAIN C OF SERINE/THREONINE-PROTEIN KINASE PAK 4
ChainResidue
ASER331
AGLN358
AARG359
ATHR404
ASER443
AASP444
APHE461
ALEU475
AVAL476
AGLY477
ATYR480
ATRP481
AGLU507

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR CHAIN D OF SERINE/THREONINE-PROTEIN KINASE PAK 4
ChainResidue
BSER331
BARG359
BTHR404
BASP444
BLEU475
BVAL476
BGLY477
BPRO479
BTYR480
BTRP481
BGLU507
BPHE516

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 Residues50
DetailsRegion: {"description":"GEF-interaction domain (GID)"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
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 Residues8
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 Residues2
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

246031

PDB entries from 2025-12-10

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