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1UU3

Structure of human PDK1 kinase domain in complex with LY333531

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A1367
ChainResidue
ALYS76
AARG131
ATHR148
APHE149
AGLN150
AHOH2274
AHOH2275

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A1368
ChainResidue
ASER160
AGLN220
AGOL1359
AHOH2161
AHOH2276
ALYS144
ATYR146

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A1369
ChainResidue
AARG106
APRO140
ALYS144
AHIS351
AGOL1359
ASO41373
AHOH2277
AHOH2278
AHOH2279

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1370
ChainResidue
ALYS83
AVAL345
ATHR346
ATRP347
AGLU348

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1371
ChainResidue
AGLY91
ASER92
APHE93
ASER94
AGOL1360
ALY41374

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1372
ChainResidue
AARG75
AARG136
ALYS199

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A1373
ChainResidue
AARG106
AGLU107
AHIS351
AGLN352
AGOL1359
ASO41369
AHOH2042
AHOH2281
AHOH2282

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE LY4 A1374
ChainResidue
ALEU88
AGLY89
AALA109
ALYS111
AGLU130
AVAL143
ALEU159
ASER160
ATYR161
AALA162
AGLY165
AGLU166
AGLU209
AASN210
ALEU212
ATHR222
AASP223
AGOL1366
ASO41371

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A1359
ChainResidue
AARG106
AGLU107
ATYR108
ATYR161
ASO41368
ASO41369
ASO41373
AHOH2104
AHOH2278

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1360
ChainResidue
ALYS111
ALEU113
ATYR126
AVAL127
AGLU130
ASO41371

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1361
ChainResidue
APRO79
ALYS154
ATYR156
AGLU328
AGLU331
AGLY332
AHOH2268

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1362
ChainResidue
ALYS76
APHE147
ATHR148
AHOH2092

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A1363
ChainResidue
ALEU297
ATYR299
APHE301

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A1364
ChainResidue
ATRP347
AGLU348
AASN349
ALEU350
AHIS351
AALA103
ATHR104
ASER105
AHIS139
ASER191

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A1365
ChainResidue
APHE82
ALYS83
APHE84
AGLU194
AGLY334
ALYS337
AHOH2269
AHOH2270
AHOH2273

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A1366
ChainResidue
AGLY89
AGLU90
ALY41374
AHOH2021
AHOH2109

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

218853

PDB entries from 2024-04-24

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