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2XCK

Crystal structure of PDK1 in complex with a pyrazoloquinazoline inhibitor

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 Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1361
ChainResidue
AALA103
AHOH2057
ATHR104
AHIS139
ASER191
ATRP347
AGLU348
AASN349
ALEU350
AHIS351

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1362
ChainResidue
APHE82
ALYS83
APHE84
AGLU194
AGLY334
ALYS337
AHOH2139

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1363
ChainResidue
AARG106
AGLU107
ATYR146
ASER160
ATYR161
AGOL1365
ASO41370

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1365
ChainResidue
AARG106
AGLU107
AHIS351
AGLN352
AGOL1363
ASO41370

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1368
ChainResidue
ALYS76
AARG131
ATHR148
APHE149
AGLN150

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1369
ChainResidue
ALYS144
ALYS144
ATYR146
ATYR146

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1370
ChainResidue
AARG106
AHIS351
AGOL1363
AGOL1365

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MH4 A 1360
ChainResidue
ALEU88
AGLY91
ASER94
AALA109
ALYS111
ALEU159
ASER160
AALA162
ALEU212
ATHR222
AASP223
AHOH2136

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSTTVlArelatsre..........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
ATHR255

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883
ChainResidueDetails
APHE142
ATYR161
AASN210
AASP216
ATYR273

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22999883
ChainResidueDetails
AALA259

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC and INSR => ECO:0000269|PubMed:11481331, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16314505
ChainResidueDetails
AARG59

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10455013
ChainResidueDetails
AARG75

site_idSWS_FT_FI6
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
APHE291

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0
ChainResidueDetails
ATHR354

217705

PDB entries from 2024-03-27

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