eF-site ID 1uwh-AB PDB Code 1uwh Chain A, B click to enlarge Title The complex of wild type B-RAF and BAY439006. Classification TRANSFERASE Compound B-RAF PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE Source null (BRAF_HUMAN) Sequence A:  DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNV TAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTAPQLAI VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYL HAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVLSGSILW MAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNI NNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKK KRDERPLFPQILASIELLARSLPK B:  DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNV TAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTAPQLAI VTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYL HAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVLSGSILW MAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNI NNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKK KRDERPLFPQILASIELLARSLPK Description Functional site 1) chain A residue 449 type sequence W description BINDING SITE FOR RESIDUE CL B 1724 source : AC1 2) chain A residue 508 type sequence R description BINDING SITE FOR RESIDUE CL B 1724 source : AC1 3) chain B residue 449 type sequence W description BINDING SITE FOR RESIDUE CL B 1724 source : AC1 4) chain B residue 508 type sequence R description BINDING SITE FOR RESIDUE CL B 1724 source : AC1 5) chain A residue 462 type sequence I description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 6) chain A residue 470 type sequence V description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 7) chain A residue 480 type sequence A description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 8) chain A residue 500 type sequence E description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 9) chain A residue 504 type sequence L description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 10) chain A residue 513 type sequence L description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 11) chain A residue 528 type sequence T description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 12) chain A residue 529 type sequence Q description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 13) chain A residue 530 type sequence W description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 14) chain A residue 531 type sequence C description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 15) chain A residue 566 type sequence L description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 16) chain A residue 573 type sequence H description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 17) chain A residue 582 type sequence F description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 18) chain A residue 591 type sequence I description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 19) chain A residue 592 type sequence G description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 20) chain A residue 593 type sequence D description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 21) chain A residue 594 type sequence F description BINDING SITE FOR RESIDUE BAX A 1723 source : AC2 22) chain B residue 462 type sequence I description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 23) chain B residue 470 type sequence V description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 24) chain B residue 480 type sequence A description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 25) chain B residue 500 type sequence E description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 26) chain B residue 504 type sequence L description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 27) chain B residue 513 type sequence L description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 28) chain B residue 528 type sequence T description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 29) chain B residue 529 type sequence Q description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 30) chain B residue 530 type sequence W description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 31) chain B residue 531 type sequence C description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 32) chain B residue 566 type sequence L description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 33) chain B residue 573 type sequence H description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 34) chain B residue 582 type sequence F description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 35) chain B residue 591 type sequence I description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 36) chain B residue 592 type sequence G description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 37) chain B residue 593 type sequence D description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 38) chain B residue 594 type sequence F description BINDING SITE FOR RESIDUE BAX B 1723 source : AC3 39) chain A residue 576 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 576 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 463 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 463 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 483 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 483 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 447 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 447 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 671 type MOD_RES sequence G description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 671 type MOD_RES sequence G description Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714 source Swiss-Prot : SWS_FT_FI4 49) chain A residue 578 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581 source Swiss-Prot : SWS_FT_FI5 50) chain B residue 578 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581 source Swiss-Prot : SWS_FT_FI5 51) chain A residue 462-482 type prosite sequence IGSGSFGTVYKGKWHGDVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK source prosite : PS00107 52) chain A residue 571-583 type prosite sequence IIHRDLKSNNIFL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL source prosite : PS00108

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