eF-site ID 4q5j-B PDB Code 4q5j Chain B click to enlarge Title Crystal structure of SeMet derivative BRI1 in complex with BKI1 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Protein BRASSINOSTEROID INSENSITIVE 1 Source (BKI1_ARATH) Sequence B:  DLEVLFQGPHXPLRKLTFADLLQATNGFHNDSLIGSGGFG DVYKAILKDGSAVAIKKLIHDREFXAEXETIGKIKHRNLV PLLGYCKVGDERLLVYEFXKYGSLEDVLHVKLNWSTRRKI AIGSARGLAFLHHNCSPHIIHRDXKSSNVLLDENLEARVS DFGXARLXSAXDXHLXVXTLAGTPGYVPPEYYQXFRCSTK GDVYSYGVVLLELLTGKRPTDSPDFGDNNLVGWVKQHAKL RISDVFDPELXKEDPALEIELLQHLKVAVACLDDRAWRRP TXVQVXAXFKEIQA Description Functional site 1) chain B residue 892 type sequence G description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 2) chain B residue 893 type sequence G description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 3) chain B residue 897 type sequence V description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 4) chain B residue 909 type sequence A description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 5) chain B residue 911 type sequence K description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 6) chain B residue 957 type sequence E description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 7) chain B residue 959 type sequence X description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 8) chain B residue 962 type sequence G description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 9) chain B residue 963 type sequence S description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 10) chain B residue 966 type sequence D description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 11) chain B residue 1011 type sequence K description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 12) chain B residue 1013 type sequence S description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 13) chain B residue 1014 type sequence N description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 14) chain B residue 1016 type sequence L description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 15) chain B residue 1027 type sequence D description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 16) chain B residue 880 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 17) chain B residue 982 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 18) chain B residue 887 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19105183 source Swiss-Prot : SWS_FT_FI6 19) chain B residue 1044 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:Q9M0G7, ECO:0000255 source Swiss-Prot : SWS_FT_FI10 20) chain B residue 1052 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:C0LGT6 source Swiss-Prot : SWS_FT_FI11 21) chain B residue 1072 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000255 source Swiss-Prot : SWS_FT_FI12 22) chain B residue 1035 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 23) chain B residue 1042 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 24) chain B residue 1060 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 25) chain B residue 891 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 26) chain B residue 981 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 27) chain B residue 956 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:19124768 source Swiss-Prot : SWS_FT_FI8 28) chain B residue 1039 type MOD_RES sequence X description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 29) chain B residue 1045 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 30) chain B residue 1049 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 31) chain B residue 1009 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 B residue 889 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 1027 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 911 type BINDING sequence K description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 957 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 36) chain B residue 963 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 1009 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 872 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:11027724, ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links