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4AW0

Human PDK1 Kinase Domain in Complex with Allosteric Compound PS182 Bound to the PIF-Pocket

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 Residues22
DetailsBINDING SITE FOR RESIDUE ATP A 500
ChainResidue
AGLY89
AGLU166
ALEU212
AASP223
AMG800
AMG850
AHOH2017
AHOH2019
AHOH2020
AHOH2021
AHOH2136
AGLY91
AHOH2137
AHOH2138
AHOH2232
ASER92
ASER94
AVAL96
AALA109
ALYS111
ASER160
AALA162

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MJF A 600
ChainResidue
ALYS76
AVAL127
ATHR128
AARG131
ATHR148
APHE149
AGLN150
ALEU155
ATYR156
AHOH2072

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DMS A 700
ChainResidue
ATHR104
ASER105
AHIS139
ASER191
ATRP347
AGLU348
AASN349
ALEU350
AHIS351

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 800
ChainResidue
ALYS111
AASP223
AATP500
AMG850

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 850
ChainResidue
AASN210
AASP223
AATP500
AMG800
AHOH2130

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DTD A 900
ChainResidue
APHE242
AVAL243
AGLY244
AALA246
AVAL249
AARG283
AGLU287
AHOH2177

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
ALYS111
ASER160
AGLU166
AASP223
ASER92

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 2024-04-17

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