eF-site ID 3e8d-B PDB Code 3e8d Chain B 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 B:  KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRK EVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRL CFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEY LHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGA TMKXFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLL KKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPP FKPQVTSEVDTRYFDDEFTAQSIQRTHFPQFDYSASIR Description Functional site 1) chain B residue 161 type sequence G description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 2) chain B residue 164 type sequence G description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 3) chain B residue 166 type sequence V description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 4) chain B residue 179 type sequence A description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 5) chain B residue 181 type sequence K description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 6) chain B residue 200 type sequence E description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 7) chain B residue 204 type sequence L description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 8) chain B residue 227 type sequence F description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 9) chain B residue 229 type sequence M description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 10) chain B residue 230 type sequence E description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 11) chain B residue 231 type sequence Y description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 12) chain B residue 232 type sequence A description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 13) chain B residue 280 type sequence N description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 14) chain B residue 282 type sequence M description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 15) chain B residue 292 type sequence T description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 16) chain B residue 293 type sequence D description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 17) chain B residue 294 type sequence F description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 18) chain B residue 439 type sequence F description BINDING SITE FOR RESIDUE G98 B 1 source : AC2 19) chain B residue 280 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12434148 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 293 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12434148 source Swiss-Prot : SWS_FT_FI3 21) chain B 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 22) chain B residue 306 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 23) chain B residue 313 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 24) chain B residue 158 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 181 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 26) chain B 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 27) chain B residue 447 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI5 28) chain B residue 478 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI5

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