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4JDK

Crystal structure of Serine/threonine-protein kinase PAK 4 F461V mutant in complex with Paktide S peptide substrate

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 Residues22
DetailsBINDING SITE FOR CHAIN B OF PAKTIDE S
ChainResidue
ASER331
AASP444
AVAL461
ALEU475
AGLY477
ATHR478
APRO479
ATYR480
ATRP481
AGLU507
APHE516
AGLN357
ALEU521
AMET524
BHOH101
AGLN358
AARG359
ALEU362
ATHR404
AASP440
ALYS442
ASER443

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP440

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU
ChainResidueDetails
AILE327
ALYS350

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU
ChainResidueDetails
AASP458
AGLU396

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER291

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|Ref.32, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASEP474

221051

PDB entries from 2024-06-12

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