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3WF7

Crystal structure of S6K1 kinase domain in complex with a purine derivative 1-(9H-purin-6-yl)-N-[3-(trifluoromethyl)phenyl]piperidine-4-carboxamide

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS240
AHIS245
AHIS251
ACYS254

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FS9 A 402
ChainResidue
AVAL105
AALA121
ALYS123
ALEU125
AVAL156
AGLU173
ATYR174
ALEU175
AMET225
ALYS241
AHOH560
AHOH563
AHOH696
ALYS99
AGLY100
ATYR102
AGLY103
ALYS104

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ATYR174
ASER176
ALYS329
AASN331
ASER334
AHOH539
AHOH595
AHOH600

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGYGKVFqVrkvtgantgki.......FAMK
ChainResidueDetails
ALEU97-LYS123

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNIML
ChainResidueDetails
AILE214-LEU226

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
AASP218

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU97
ALYS123

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:19864428, ECO:0000269|PubMed:9445476
ChainResidueDetails
ATPO252

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19085255
ChainResidueDetails
ASER394

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PDB entries from 2024-05-01

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