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2PE0

CRYSTAL STRUCTURE OF HUMAN PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1 (PDK1) 5-Hydroxy-3-[1-(1H-pyrrol-2-yl)-eth-(Z)-ylidene]-1,3-dihydro-indol-2-one COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
ALYS76
AARG131
ATHR148
APHE149
AGLN150
AHOH740

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
AARG106
APRO140
AHIS351

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 39Z A 501
ChainResidue
ALEU88
AALA109
ASER160
ATYR161
AALA162
ALEU212
ATHR222
AHOH796

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
AGLY91
ASER92
APHE93
ASER94
ALYS111
AASP223

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
APHE82
ALYS83
APHE84
ALYS337

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 604
ChainResidue
AALA103
ATHR104
AHIS139
ATRP347
AGLU348
AASN349
ALEU350
AHIS351

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSTVVlArelatsre..........YAIK
ChainResidueDetails
ALEU88-LYS111

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNILL
ChainResidueDetails
AILE201-LEU213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP205

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883
ChainResidueDetails
ASER92
ALYS111
ASER160
AGLU166
AASP223

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22999883
ChainResidueDetails
AGLU209

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10455013, ECO:0000269|PubMed:11481331, ECO:0000269|PubMed:15772071, ECO:0000269|PubMed:16780920, ECO:0000269|Ref.8
ChainResidueDetails
ASEP241

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0
ChainResidueDetails
ALYS304

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756
ChainResidueDetails
ATHR354

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PDB entries from 2024-04-24

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