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5ACK

Human PDK1 Kinase Domain in Complex with Allosteric Compound 7 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 Residues21
DetailsBINDING SITE FOR RESIDUE ATP A 500
ChainResidue
AGLY89
AALA162
AGLU166
ALEU212
ANA900
ANA902
AHOH2020
AHOH2022
AHOH2189
AHOH2190
AHOH2330
AGLU90
AHOH2331
AHOH2332
AGLY91
ASER92
ASER94
AVAL96
AALA109
ASER160
ATYR161

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SVQ A 600
ChainResidue
ALYS115
AVAL127
AARG131
ATHR148
APHE149
AGLN150
ALEU155

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DTD A 700
ChainResidue
APHE242
AVAL243
AGLY244
AGLU287
APHE291
AHOH2221

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DMS A 800
ChainResidue
ATHR104
ASER105
AHIS139
APHE141
ATRP347
AASN349
ALEU350
AHIS351
AHOH2027

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 900
ChainResidue
AASP223
AATP500
ANA902
AHOH2022

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 901
ChainResidue
AGLY244
ATHR245
AHOH2220
AHOH2221

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 902
ChainResidue
AASN210
AASP223
AATP500
ANA900
AHOH2181

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 2024-07-24

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