eF-site ID 1opl-AB PDB Code 1opl Chain A, 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 null (ABL1_HUMAN) Sequence A:  DPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCE AQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLL SSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASD GKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRN KPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVW KKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQL LGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLL YMATQISSAMEYLEKKNFIHRNLAARNCLVGENHLVKVAD FGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSD VWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERP EGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESS ISDEVEKELGK B:  SLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQ RSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVH HHSTVADGLITTLHYPAPDKWEMERTDITMKHKLGGGQYG EVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIK HPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQE VNAVVLLYMATQISSAMEYLEKKNFIHRNLAARNCLVGEN HLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYN KFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEK DYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFE TMFQE Description Functional site 1) chain A residue 360 type sequence L description BINDING SITE FOR RESIDUE MYR A 538 source : AC1 2) chain A residue 481 type sequence E description BINDING SITE FOR RESIDUE MYR A 538 source : AC1 3) chain A residue 521 type sequence I description BINDING SITE FOR RESIDUE MYR A 538 source : AC1 4) chain A residue 529 type sequence L description BINDING SITE FOR RESIDUE MYR A 538 source : AC1 5) chain A residue 272 type sequence Y description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 6) chain A residue 275 type sequence V description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 7) chain A residue 288 type sequence A description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 8) chain A residue 290 type sequence K description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 9) chain A residue 305 type sequence E description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 10) chain A residue 309 type sequence M description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 11) chain A residue 332 type sequence I description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 12) chain A residue 334 type sequence T description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 13) chain A residue 335 type sequence E description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 14) chain A residue 337 type sequence M description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 15) chain A residue 340 type sequence G description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 16) chain A residue 389 type sequence L description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 17) chain A residue 399 type sequence A description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 18) chain A residue 400 type sequence D description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 19) chain A residue 401 type sequence F description BINDING SITE FOR RESIDUE P16 A 539 source : AC2 20) chain B residue 272 type sequence Y description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 21) chain B residue 305 type sequence E description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 22) chain B residue 309 type sequence M description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 23) chain B residue 334 type sequence T description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 24) chain B residue 335 type sequence E description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 25) chain B residue 337 type sequence M description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 26) chain B residue 340 type sequence G description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 27) chain B residue 389 type sequence L description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 28) chain B residue 399 type sequence A description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 29) chain B residue 401 type sequence F description BINDING SITE FOR RESIDUE P16 B 538 source : AC3 30) chain B residue 229 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P42684 source Swiss-Prot : SWS_FT_FI8 31) chain A residue 229 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P42684 source Swiss-Prot : SWS_FT_FI8 32) chain A residue 257 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 33) chain A residue 413 type MOD_RES sequence T description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 34) chain B residue 253 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 35) chain B residue 257 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 36) chain A residue 253 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 37) chain B residue 413 type MOD_RES sequence T description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 38) 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 39) chain A 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 40) chain A residue 446 type MOD_RES sequence V description Phosphoserine => ECO:0000250|UniProtKB:P00520 source Swiss-Prot : SWS_FT_FI11 41) chain B residue 446 type MOD_RES sequence V description Phosphoserine => ECO:0000250|UniProtKB:P00520 source Swiss-Prot : SWS_FT_FI11 42) chain A residue 248 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI2 43) chain A residue 271 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 44) chain A residue 316 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 45) chain B residue 271 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 46) chain B residue 316 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 47) chain B residue 172 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 48) chain B residue 185 type MOD_RES sequence R description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 49) chain B residue 215 type MOD_RES sequence A description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 115 type MOD_RES sequence N description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 128 type MOD_RES sequence G description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 52) chain A residue 139 type MOD_RES sequence N description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 53) chain A residue 172 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 54) chain A residue 185 type MOD_RES sequence R description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 55) chain A residue 215 type MOD_RES sequence A description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 56) chain A residue 226 type MOD_RES sequence D description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI7 57) chain B residue 226 type MOD_RES sequence D description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI7 58) chain A residue 267-290 type prosite sequence LGGGQYGEVYEGVWKKYSLTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK source prosite : PS00107 59) chain A 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 60) 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

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