eF-site ID 1opl-B PDB Code 1opl Chain B click to enlarge Title Structural basis for the auto-inhibition of c-Abl tyrosine kinase Classification TRANSFERASE Compound proto-oncogene tyrosine-protein kinase Source Homo sapiens (Human) (ABL1_HUMAN) Sequence B:  SLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQ RSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVH HHSTVADGLITTLHYPAPDKWEMERTDITMKHKLGGGQYG EVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIK HPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQE VNAVVLLYMATQISSAMEYLEKKNFIHRNLAARNCLVGEN HLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYN KFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEK DYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFE TMFQE Description Functional site 1) chain B residue 272 type sequence Y description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 2) chain B residue 305 type sequence E description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 3) chain B residue 309 type sequence M description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 4) chain B residue 334 type sequence T description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 5) chain B residue 335 type sequence E description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 6) chain B residue 337 type sequence M description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 7) chain B residue 340 type sequence G description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 8) chain B residue 389 type sequence L description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 9) chain B residue 399 type sequence A description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 10) chain B residue 401 type sequence F description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 11) chain B residue 363 type ACT_SITE sequence A description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 12) chain B residue 271 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 13) chain B residue 316 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 14) chain B residue 229 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P42684 source Swiss-Prot : SWS_FT_FI8 15) chain B residue 226 type MOD_RES sequence D description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI7 16) chain B residue 393 type MOD_RES sequence N description Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI10 17) chain B residue 446 type MOD_RES sequence V description Phosphoserine => ECO:0000250|UniProtKB:P00520 source Swiss-Prot : SWS_FT_FI11 18) chain B residue 172 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 19) chain B residue 185 type MOD_RES sequence R description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 20) chain B residue 215 type MOD_RES sequence A description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 21) chain B residue 253 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 22) chain B residue 257 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 23) chain B residue 413 type MOD_RES sequence T description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9

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