eF-site ID 4ejn-A PDB Code 4ejn Chain A click to enlarge Title Crystal structure of autoinhibited form of AKT1 in complex with N-(4-(5-(3-acetamidophenyl)-2-(2-aminopyridin-3-yl)-3H-imidazo[4,5-b]pyridin-3-yl)benzyl)-3-fluorobenzamide Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound RAC-alpha serine/threonine-protein kinase Source Homo sapiens (Human) (AKT1_HUMAN) Sequence A:  VAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPA PLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHV ETPEEREEWTTAIQTVADGRVTMNEFEYLKLLGKGTFGKV ILVKEKATGRYYAMKILKKEVIVVLQNSRHPFLTALKYSF QTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEI VSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCK EGIKKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM MCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSG LLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLS PPFKPQVTSETDTRYF Description (1)  RAC-alpha serine/threonine-protein kinase (E.C.2.7.11.1) Functional site 1) chain A residue 53 type sequence N description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 2) chain A residue 54 type sequence N description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 3) chain A residue 59 type sequence Q description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 4) chain A residue 78 type sequence L description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 5) chain A residue 79 type sequence Q description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 6) chain A residue 80 type sequence W description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 7) chain A residue 84 type sequence I description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 8) chain A residue 210 type sequence L description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 9) chain A residue 211 type sequence T description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 10) chain A residue 270 type sequence V description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 11) chain A residue 271 type sequence V description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 12) chain A residue 272 type sequence Y description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 13) chain A residue 273 type sequence R description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 14) chain A residue 274 type sequence D description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 15) chain A residue 290 type sequence I description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 16) chain A residue 292 type sequence D description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 17) chain A residue 326 type sequence Y description BINDING SITE FOR RESIDUE 0R4 A 501 source : AC1 18) chain A residue 163 type sequence K description BINDING SITE FOR RESIDUE SBT A 502 source : AC2 19) chain A residue 147 type sequence M description BINDING SITE FOR RESIDUE EDO A 503 source : AC3 20) chain A residue 222 type sequence R description BINDING SITE FOR RESIDUE EDO A 503 source : AC3 21) chain A residue 270-282 type prosite sequence VVYRDLKLENLML description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDLKleNLML source prosite : PS00108 22) chain A residue 274 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 312 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000269|PubMed:22629392 source Swiss-Prot : SWS_FT_FI11 24) 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_FI12 25) chain A residue 14 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:12964941 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 23 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:12964941 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 53 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:12964941 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 86 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12176338, ECO:0000269|PubMed:12964941 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 156 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 179 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 14 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21775285 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 20 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21775285 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 176 type MOD_RES sequence Y description Phosphotyrosine; by TNK2 => ECO:0000269|PubMed:20333297 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 308 type MOD_RES sequence T 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_FI9

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