eF-site ID 1iep-AB PDB Code 1iep Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF THE C-ABL KINASE DOMAIN IN COMPLEX WITH STI-571. Classification TRANSFERASE Compound PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL Source null (ABL1_MOUSE) Sequence A:  MDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKY SLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGV CTREPPFYIITEFMTYGNLLDYLRECNRQEVSAVVLLYMA TQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGL SRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWA FGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGC PEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQ B:  MDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKY SLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGV CTREPPFYIITEFMTYGNLLDYLRECNRQEVSAVVLLYMA TQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGL SRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWA FGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGC PEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQ Description Functional site 1) chain A residue 360 type sequence I description BINDING SITE FOR RESIDUE CL A 2 source : AC2 2) chain B residue 360 type sequence I description BINDING SITE FOR RESIDUE CL B 3 source : AC3 3) chain A residue 319 type sequence T description BINDING SITE FOR RESIDUE CL A 4 source : AC4 4) chain A residue 372 type sequence G description BINDING SITE FOR RESIDUE CL A 4 source : AC4 5) chain A residue 253 type sequence Y description BINDING SITE FOR RESIDUE CL A 5 source : AC5 6) chain A residue 321 type sequence G description BINDING SITE FOR RESIDUE CL A 5 source : AC5 7) chain A residue 322 type sequence N description BINDING SITE FOR RESIDUE CL A 5 source : AC5 8) chain B residue 253 type sequence Y description BINDING SITE FOR RESIDUE CL B 6 source : AC6 9) chain B residue 321 type sequence G description BINDING SITE FOR RESIDUE CL B 6 source : AC6 10) chain B residue 322 type sequence N description BINDING SITE FOR RESIDUE CL B 6 source : AC6 11) chain A residue 248 type sequence L description BINDING SITE FOR RESIDUE STI A 201 source : AC7 12) chain A residue 253 type sequence Y description BINDING SITE FOR RESIDUE STI A 201 source : AC7 13) chain A residue 269 type sequence A description BINDING SITE FOR RESIDUE STI A 201 source : AC7 14) chain A residue 271 type sequence K description BINDING SITE FOR RESIDUE STI A 201 source : AC7 15) chain A residue 286 type sequence E description BINDING SITE FOR RESIDUE STI A 201 source : AC7 16) chain A residue 290 type sequence M description BINDING SITE FOR RESIDUE STI A 201 source : AC7 17) chain A residue 299 type sequence V description BINDING SITE FOR RESIDUE STI A 201 source : AC7 18) chain A residue 313 type sequence I description BINDING SITE FOR RESIDUE STI A 201 source : AC7 19) chain A residue 315 type sequence T description BINDING SITE FOR RESIDUE STI A 201 source : AC7 20) chain A residue 317 type sequence F description BINDING SITE FOR RESIDUE STI A 201 source : AC7 21) chain A residue 318 type sequence M description BINDING SITE FOR RESIDUE STI A 201 source : AC7 22) chain A residue 360 type sequence I description BINDING SITE FOR RESIDUE STI A 201 source : AC7 23) chain A residue 361 type sequence H description BINDING SITE FOR RESIDUE STI A 201 source : AC7 24) chain A residue 362 type sequence R description BINDING SITE FOR RESIDUE STI A 201 source : AC7 25) chain A residue 380 type sequence A description BINDING SITE FOR RESIDUE STI A 201 source : AC7 26) chain A residue 381 type sequence D description BINDING SITE FOR RESIDUE STI A 201 source : AC7 27) chain A residue 382 type sequence F description BINDING SITE FOR RESIDUE STI A 201 source : AC7 28) chain B residue 248 type sequence L description BINDING SITE FOR RESIDUE STI B 202 source : AC8 29) chain B residue 253 type sequence Y description BINDING SITE FOR RESIDUE STI B 202 source : AC8 30) chain B residue 256 type sequence V description BINDING SITE FOR RESIDUE STI B 202 source : AC8 31) chain B residue 269 type sequence A description BINDING SITE FOR RESIDUE STI B 202 source : AC8 32) chain B residue 271 type sequence K description BINDING SITE FOR RESIDUE STI B 202 source : AC8 33) chain B residue 286 type sequence E description BINDING SITE FOR RESIDUE STI B 202 source : AC8 34) chain B residue 290 type sequence M description BINDING SITE FOR RESIDUE STI B 202 source : AC8 35) chain B residue 299 type sequence V description BINDING SITE FOR RESIDUE STI B 202 source : AC8 36) chain B residue 313 type sequence I description BINDING SITE FOR RESIDUE STI B 202 source : AC8 37) chain B residue 315 type sequence T description BINDING SITE FOR RESIDUE STI B 202 source : AC8 38) chain B residue 318 type sequence M description BINDING SITE FOR RESIDUE STI B 202 source : AC8 39) chain B residue 360 type sequence I description BINDING SITE FOR RESIDUE STI B 202 source : AC8 40) chain B residue 361 type sequence H description BINDING SITE FOR RESIDUE STI B 202 source : AC8 41) chain B residue 380 type sequence A description BINDING SITE FOR RESIDUE STI B 202 source : AC8 42) chain B residue 381 type sequence D description BINDING SITE FOR RESIDUE STI B 202 source : AC8 43) chain B residue 382 type sequence F description BINDING SITE FOR RESIDUE STI B 202 source : AC8 44) chain A residue 363 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 363 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 248 type BINDING sequence L description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 248 type BINDING sequence L description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 316 type BINDING sequence E description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 316 type BINDING sequence E description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 229 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P42684 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 229 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P42684 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 253 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P00519 source Swiss-Prot : SWS_FT_FI5 53) chain A residue 257 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P00519 source Swiss-Prot : SWS_FT_FI5 54) chain A residue 413 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P00519 source Swiss-Prot : SWS_FT_FI5 55) chain B residue 253 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P00519 source Swiss-Prot : SWS_FT_FI5 56) chain B residue 257 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P00519 source Swiss-Prot : SWS_FT_FI5 57) chain B residue 413 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P00519 source Swiss-Prot : SWS_FT_FI5 58) chain A residue 393 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290 source Swiss-Prot : SWS_FT_FI6 59) chain B residue 393 type MOD_RES sequence Y description Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290 source Swiss-Prot : SWS_FT_FI6 60) chain A residue 446 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:9109492 source Swiss-Prot : SWS_FT_FI7 61) chain B residue 446 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:9109492 source Swiss-Prot : SWS_FT_FI7 62) chain A residue 248-271 type prosite sequence LGGGQYGEVYEGVWKKYSLTVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK source prosite : PS00107 63) chain A residue 359-371 type prosite sequence FIHRDLAARNCLV description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV source prosite : PS00109 64) chain A residue 271 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 65) chain B residue 271 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3

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