eF-site ID 4gv1-A PDB Code 4gv1 Chain A click to enlarge Title PKB alpha in complex with AZD5363 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound RAC-alpha serine/threonine-protein kinase Source Homo sapiens (Human) (AKT1_HUMAN) Sequence A:  SRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILK KEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDR LCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALD YLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKD GATMKXFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM MCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSG LLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLS PPFKPQVTSETDTRYFDEEFTAQMITITPSMECVDSERRP HFPQFDYSAS Description (1)  RAC-alpha serine/threonine-protein kinase (E.C.2.7.11.1) Functional site 1) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 2) chain A residue 158 type sequence K description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 3) chain A residue 159 type sequence G description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 4) chain A residue 162 type sequence G description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 5) chain A residue 163 type sequence K description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 6) chain A residue 164 type sequence V description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 7) chain A residue 177 type sequence A description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 8) chain A residue 179 type sequence K description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 9) chain A residue 181 type sequence L description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 10) chain A residue 227 type sequence M description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 11) chain A residue 228 type sequence E description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 12) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 13) chain A residue 234 type sequence E description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 14) chain A residue 278 type sequence E description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 15) chain A residue 281 type sequence M description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 16) chain A residue 292 type sequence D description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 17) chain A residue 438 type sequence F description BINDING SITE FOR RESIDUE 0XZ A 501 source : AC1 18) chain A residue 154 type sequence K description BINDING SITE FOR RESIDUE GOL A 502 source : AC2 19) chain A residue 434 type sequence D description BINDING SITE FOR RESIDUE GOL A 502 source : AC2 20) chain A residue 435 type sequence T description BINDING SITE FOR RESIDUE GOL A 502 source : AC2 21) chain A residue 436 type sequence R description BINDING SITE FOR RESIDUE GOL A 502 source : AC2 22) chain A residue 179 type sequence K description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 23) chain A residue 186 type sequence I description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 24) chain A residue 191 type sequence E description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 25) chain A residue 195 type sequence T description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 26) chain A residue 198 type sequence E description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 27) chain A residue 292 type sequence D description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 28) chain A residue 294 type sequence G description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 29) chain A residue 309 type sequence F description BINDING SITE FOR RESIDUE GOL A 504 source : AC4 30) chain A residue 310 type sequence C description BINDING SITE FOR RESIDUE GOL A 504 source : AC4 31) chain A residue 311 type sequence G description BINDING SITE FOR RESIDUE GOL A 504 source : AC4 32) chain A residue 312 type sequence T description BINDING SITE FOR RESIDUE GOL A 504 source : AC4 33) chain A residue 313 type sequence P description BINDING SITE FOR RESIDUE GOL A 504 source : AC4 34) chain A residue 316 type sequence L description BINDING SITE FOR RESIDUE GOL A 504 source : AC4 35) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE GOL A 505 source : AC5 36) chain A residue 158 type sequence K description BINDING SITE FOR RESIDUE GOL A 505 source : AC5 37) chain A residue 234 type sequence E description BINDING SITE FOR RESIDUE GOL A 505 source : AC5 38) chain A residue 236 type sequence F description BINDING SITE FOR RESIDUE GOL A 505 source : AC5 39) chain A residue 442 type sequence F description BINDING SITE FOR RESIDUE GOL A 505 source : AC5 40) chain A residue 156-189 type prosite sequence LGKGTFGKVILVKEKATGRYYAMKILKKEVIVAK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVkekatgryyamkilkkevIVAK source prosite : PS00107 41) chain A residue 270-282 type prosite sequence VVYRDLKLENLML description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDLKleNLML source prosite : PS00108 42) 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 43) chain A residue 473 type CARBOHYD sequence D description O-linked (GlcNAc) serine; alternate => ECO:0000250|UniProtKB:P31750 source Swiss-Prot : SWS_FT_FI10 44) 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 45) chain A residue 156 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 179 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 462 type SITE sequence D description Cleavage; by caspase-3 => ECO:0000250|UniProtKB:P31750 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 176 type MOD_RES sequence Y description Phosphotyrosine; by TNK2 => ECO:0000269|PubMed:20333297 source Swiss-Prot : SWS_FT_FI4 49) 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 50) chain A residue 448 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 450 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 52) 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 53) chain A residue 474 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:12149249 source Swiss-Prot : SWS_FT_FI8 54) chain A residue 305 type CARBOHYD sequence T description O-linked (GlcNAc) threonine => ECO:0000269|PubMed:22629392 source Swiss-Prot : SWS_FT_FI9 55) 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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