eF-site ID 3wf7-A PDB Code 3wf7 Chain A click to enlarge Title Crystal structure of S6K1 kinase domain in complex with a purine derivative 1-(9H-purin-6-yl)-N-[3-(trifluoromethyl)phenyl]piperidine-4-carboxamide Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Ribosomal protein S6 kinase beta-1 Source Homo sapiens (Human) (KS6B1_HUMAN) Sequence A:  PEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAM KVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAF QTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEI SMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKE SIHDTHXFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYD MLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLK KLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKV EPPFKPLLQ Description (1)  Ribosomal protein S6 kinase beta-1 (E.C.2.7.11.1) Functional site 1) chain A residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 2) chain A residue 245 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 3) chain A residue 251 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 4) chain A residue 254 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC1 5) chain A residue 99 type sequence K description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 6) chain A residue 100 type sequence G description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 7) chain A residue 102 type sequence Y description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 8) chain A residue 103 type sequence G description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 9) chain A residue 104 type sequence K description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 10) chain A residue 105 type sequence V description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 11) chain A residue 121 type sequence A description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 12) chain A residue 123 type sequence K description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 13) chain A residue 125 type sequence L description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 14) chain A residue 156 type sequence V description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 15) chain A residue 173 type sequence E description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 16) chain A residue 174 type sequence Y description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 17) chain A residue 175 type sequence L description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 18) chain A residue 225 type sequence M description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 19) chain A residue 241 type sequence K description BINDING SITE FOR RESIDUE FS9 A 402 source : AC2 20) chain A residue 174 type sequence Y description BINDING SITE FOR RESIDUE GOL A 403 source : AC3 21) chain A residue 176 type sequence S description BINDING SITE FOR RESIDUE GOL A 403 source : AC3 22) chain A residue 329 type sequence K description BINDING SITE FOR RESIDUE GOL A 403 source : AC3 23) chain A residue 331 type sequence N description BINDING SITE FOR RESIDUE GOL A 403 source : AC3 24) chain A residue 334 type sequence S description BINDING SITE FOR RESIDUE GOL A 403 source : AC3 25) chain A residue 97-123 type prosite sequence LGKGGYGKVFQVRKVTGANTGKIFAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGYGKVFqVrkvtgantgki.......FAMK source prosite : PS00107 26) chain A residue 214-226 type prosite sequence IIYRDLKPENIML description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNIML source prosite : PS00108 27) chain A residue 218 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 97 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 123 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 252 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:19864428, ECO:0000269|PubMed:9445476 source Swiss-Prot : SWS_FT_FI3

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