eF-site ID 2fo0-A PDB Code 2fo0 Chain A click to enlarge Title Organization of the SH3-SH2 Unit in Active and Inactive Forms of the c-Abl Tyrosine Kinase Classification TRANSFERASE Compound Proto-oncogene tyrosine-protein kinase ABL1 (1B ISOFORM) Source (ABL1_HUMAN) Sequence A:  ARWNXKENLLAGPSENDPNLFVALYDFVASGDNTLSITKG EKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKH SWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISL RYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTV ADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMK HKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLK EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLD YLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRNLA ARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKW TAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDL SQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPS FAEIHQAFETMFQESSISDEVEKELG Description Functional site 1) chain A residue 481 type sequence E description BINDING SITE FOR RESIDUE MYR A 701 source : AC1 2) chain A residue 521 type sequence I description BINDING SITE FOR RESIDUE MYR A 701 source : AC1 3) chain A residue 272 type sequence Y description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 4) chain A residue 275 type sequence V description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 5) chain A residue 288 type sequence A description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 6) chain A residue 290 type sequence K description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 7) chain A residue 305 type sequence E description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 8) chain A residue 309 type sequence M description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 9) chain A residue 334 type sequence T description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 10) chain A residue 335 type sequence E description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 11) chain A residue 336 type sequence F description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 12) chain A residue 337 type sequence M description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 13) chain A residue 340 type sequence G description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 14) chain A residue 389 type sequence L description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 15) chain A residue 399 type sequence A description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 16) chain A residue 400 type sequence D description BINDING SITE FOR RESIDUE P16 A 702 source : AC2 17) chain A residue 345 type sequence Y description BINDING SITE FOR RESIDUE GOL A 703 source : AC3 18) chain A residue 391 type sequence G description BINDING SITE FOR RESIDUE GOL A 703 source : AC3 19) chain A residue 392 type sequence E description BINDING SITE FOR RESIDUE GOL A 703 source : AC3 20) chain A residue 393 type sequence N description BINDING SITE FOR RESIDUE GOL A 703 source : AC3 21) chain A residue 394 type sequence H description BINDING SITE FOR RESIDUE GOL A 703 source : AC3 22) chain A residue 197 type sequence T description BINDING SITE FOR RESIDUE GOL A 704 source : AC4 23) chain A residue 198 type sequence A description BINDING SITE FOR RESIDUE GOL A 704 source : AC4 24) chain A residue 296 type sequence T description BINDING SITE FOR RESIDUE GOL A 704 source : AC4 25) chain A residue 297 type sequence M description BINDING SITE FOR RESIDUE GOL A 704 source : AC4 26) chain A residue 382 type ACT_SITE sequence N description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 267 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 28) chain A residue 290 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 29) chain A residue 335 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 30) chain A residue 69 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:16543148, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 89 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:18775435 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 134 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 147 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 158 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 191 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 204 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 234 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 245 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI6 39) chain A residue 248 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P42684 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 267-290 type prosite sequence LGGGQYGEVYEGVWKKYSLTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK source prosite : PS00107 41) chain A residue 465 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P00520 source Swiss-Prot : SWS_FT_FI10 42) chain A residue 272 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 43) chain A residue 276 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 44) chain A residue 432 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 45) chain A residue 412 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links