eF-site ID 3cqw-AC PDB Code 3cqw Chain A, C click to enlarge Title Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor Classification TRANSFERASE Compound RAC-alpha serine/threonine-protein kinase Source null (GSK3B_HUMAN) Sequence A:  RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKK EVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRL CFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDY LHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDG ATMKXFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM CGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGL LKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSP PFKPQVTSETDTRYFDEEFTAQMIERRPHFPQFDYSASS C:  GRPRTTSFAE Description Functional site 1) chain A residue 314 type sequence E description BINDING SITE FOR RESIDUE MN A 1 source : AC1 2) chain A residue 354 type sequence H description BINDING SITE FOR RESIDUE MN A 1 source : AC1 3) chain A residue 177 type sequence A description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 4) chain A residue 211 type sequence T description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 5) chain A residue 227 type sequence M description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 6) chain A residue 228 type sequence E description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 7) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 8) chain A residue 234 type sequence E description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 9) chain A residue 278 type sequence E description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 10) chain A residue 279 type sequence N description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 11) chain A residue 281 type sequence M description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 12) chain A residue 291 type sequence T description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 13) chain A residue 292 type sequence D description BINDING SITE FOR RESIDUE CQW A 999 source : AC2 14) chain C residue 7 type MOD_RES sequence S description Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3 => ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:8250835 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 156 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 179 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 473 type CARBOHYD sequence D description O-linked (GlcNAc) serine; alternate => ECO:0000250|UniProtKB:P31750 source Swiss-Prot : SWS_FT_FI10 18) chain A residue 284 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22410793 source Swiss-Prot : SWS_FT_FI11 19) chain A residue 156-189 type prosite sequence LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVkekatgryyamkilkkevIVAK source prosite : PS00107 20) chain A residue 270-282 type prosite sequence VVYRDLKLENLML description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDLKleNLML source prosite : PS00108 21) chain A residue 176 type MOD_RES sequence Y description Phosphotyrosine; by TNK2 => ECO:0000269|PubMed:20333297 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 308 type MOD_RES sequence X description Phosphothreonine; by IKKE, PDPK1 and TBK1 => ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18456494, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9512493 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 473 type MOD_RES sequence D description Phosphoserine; by IKKE, MTOR and TBK1; alternate => ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:17013611, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20978158, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:23799035, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9736715 source Swiss-Prot : SWS_FT_FI7 24) chain A residue 474 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:12149249 source Swiss-Prot : SWS_FT_FI8 25) chain A residue 305 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000269|PubMed:22629392 source Swiss-Prot : SWS_FT_FI9 26) chain A residue 312 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000269|PubMed:22629392 source Swiss-Prot : SWS_FT_FI9

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