eF-site ID 4cqe-AB PDB Code 4cqe Chain A, B click to enlarge Title B-Raf Kinase V600E mutant in complex with a diarylthiazole B-Raf Inhibitor Classification TRANSFERASE Compound SLC45A3-BRAF FUSION PROTEIN Source (D7PBN4_HUMAN) Sequence A:  DWEIPDGQITVGQRIGSGGTVYKGKWHGDVAVKMLNVTAP TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQ WCEGSSLYHHLHASETKFEMKKLIDIARQTARGMDYLHAK SIIHRDLKSNNIFLHEDNTVKIGDFGGSILWMAPEVIRMQ NPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIEMVG RGSLSPDLSKVRSNCPKRMKRLMAECLKKKRDERPSFPRI LAEIEELARE B:  DDWEIPDGQITVGQRIGSGTVYKGKWHGDVAVKMLNVTAP TPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQ WCEGSSLYHHLHASETKFEMKKLIDIARQTARGMDYLHAK SIIHRDLKSNNIFLHEDNTVKIGDFGGSILWMAPEVIRNP YSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIEMVGRG SLSPDLSKVRSNCPKRMKRLMAECLKKKRDERPSFPRILA EIEELARE Description Functional site 1) chain A residue 471 type sequence V description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 2) chain A residue 481 type sequence A description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 3) chain A residue 483 type sequence K description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 4) chain A residue 514 type sequence L description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 5) chain A residue 516 type sequence F description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 6) chain A residue 527 type sequence I description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 7) chain A residue 529 type sequence T description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 8) chain A residue 530 type sequence Q description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 9) chain A residue 531 type sequence W description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 10) chain A residue 532 type sequence C description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 11) chain A residue 583 type sequence F description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 12) chain A residue 593 type sequence G description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 13) chain A residue 594 type sequence D description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 14) chain A residue 595 type sequence F description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 15) chain A residue 596 type sequence G description BINDING SITE FOR RESIDUE CQE A 1721 source : AC1 16) chain B residue 481 type sequence A description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 17) chain B residue 483 type sequence K description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 18) chain B residue 514 type sequence L description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 19) chain B residue 516 type sequence F description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 20) chain B residue 529 type sequence T description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 21) chain B residue 530 type sequence Q description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 22) chain B residue 531 type sequence W description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 23) chain B residue 532 type sequence C description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 24) chain B residue 583 type sequence F description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 25) chain B residue 593 type sequence G description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 26) chain B residue 594 type sequence D description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 27) chain B residue 595 type sequence F description BINDING SITE FOR RESIDUE CQE B 1721 source : AC2 28) chain A residue 671 type MOD_RES sequence R description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 671 type MOD_RES sequence R description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 576 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 576 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 463 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 483 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 463 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 483 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 578 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 578 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 463-483 type prosite sequence IGSGGTVYKGKWHGDVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK source prosite : PS00107 39) chain A residue 572-584 type prosite sequence IIHRDLKSNNIFL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL source prosite : PS00108

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