eF-site ID 3e8d-A PDB Code 3e8d Chain A click to enlarge Title Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors Classification TRANSFERASE Compound RAC-beta serine/threonine-protein kinase Source Homo sapiens (Human) (GSK3B_HUMAN) Sequence A:  KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRK EVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRL CFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEY LHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGA TMKXFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLL KKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPP FKPQVTSEVDTRYFDDEFTAQSITHFPQFDYSASIR Description Functional site 1) chain A residue 160 type sequence K description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 2) chain A residue 161 type sequence G description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 3) chain A residue 164 type sequence G description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 4) chain A residue 165 type sequence K description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 5) chain A residue 166 type sequence V description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 6) chain A residue 179 type sequence A description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 7) chain A residue 181 type sequence K description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 8) chain A residue 200 type sequence E description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 9) chain A residue 204 type sequence L description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 10) chain A residue 227 type sequence F description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 11) chain A residue 229 type sequence M description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 12) chain A residue 230 type sequence E description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 13) chain A residue 231 type sequence Y description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 14) chain A residue 232 type sequence A description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 15) chain A residue 280 type sequence N description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 16) chain A residue 282 type sequence M description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 17) chain A residue 292 type sequence T description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 18) chain A residue 293 type sequence D description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 19) chain A residue 294 type sequence F description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 20) chain A residue 439 type sequence F description BINDING SITE FOR RESIDUE G98 A 1 source : AC1 21) chain A residue 280 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12434148 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 293 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12434148 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 474 type MOD_RES sequence D description Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI7 24) chain A residue 158-191 type prosite sequence LGKGTFGKVILVREKATGRYYAMKILRKEVIIAK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVrekatgryyamkilrkevIIAK source prosite : PS00107 25) chain A residue 271-283 type prosite sequence VVYRDIKLENLML description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDIKleNLML source prosite : PS00108 26) chain A residue 306 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 27) chain A residue 313 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 28) chain A residue 158 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 181 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 309 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12434148, ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:9512493 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 447 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 478 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI5

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