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5DEW

Crystal structure of PAK1 in complex with an inhibitor compound 5

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 Residues12
Detailsbinding site for residue 59N A 601
ChainResidue
ALYS299
AHOH712
AHOH743
AHOH832
AGLU315
AMET344
AGLU345
ATYR346
ALEU347
AASP393
ALEU396
ATHR406

site_idAC2
Number of Residues14
Detailsbinding site for residue 59N B 601
ChainResidue
BALA297
BLYS299
BMET301
BMET319
BMET344
BGLU345
BTYR346
BLEU347
BASP393
BASN394
BLEU396
BTHR406
BHOH753
BHOH839

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGASGTVYtAmdvatgqe..........VAIK
ChainResidueDetails
AILE276-LYS299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:22153498
ChainResidueDetails
AASN389
BASN389

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22153498
ChainResidueDetails
AILE276
ALYS299
AGLU345
BILE276
BLYS299
BGLU345

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
ChainResidueDetails
ATYR285
BTYR285

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis, BRSK2 and PDPK1 => ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:22669945
ChainResidueDetails
AGLU423
BGLU423

222415

PDB entries from 2024-07-10

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