eF-site ID 4q5j-A PDB Code 4q5j Chain A 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 A:  DLEVLFQGPHXAFEKPLRKLTFADLLQATNGFHNDSLIGS GGFGDVYKAILKDGSAVAIKKLIHVSDREFXAEXETIGKI KHRNLVPLLGYCKVGDERLLVYEFXKYGSLEDVLKLNWST RRKIAIGSARGLAFLHHNCSPHIIHRDXKSSNVLLDENLE ARVSDFGXARLXSAXDXHLXVXTLAGTPGYVPPEYYQXFR CSTKGDVYSYGVVLLELLTGKRPTDSPDFGDNNLVGWVKQ HAKLRISDVFDPELXKEDPALEIELLQHLKVAVACLDDRA WRRPTXVQVXAXFKEIQA Description Functional site 1) chain A residue 889 type sequence I description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 2) chain A residue 891 type sequence S description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 3) chain A residue 892 type sequence G description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 4) chain A residue 893 type sequence G description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 5) chain A residue 909 type sequence A description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 6) chain A residue 911 type sequence K description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 7) chain A residue 956 type sequence Y description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 8) chain A residue 957 type sequence E description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 9) chain A residue 958 type sequence F description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 10) chain A residue 959 type sequence X description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 11) chain A residue 963 type sequence S description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 12) chain A residue 966 type sequence D description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 13) chain A residue 1011 type sequence K description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 14) chain A residue 1013 type sequence S description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 15) chain A residue 1014 type sequence N description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 16) chain A residue 1016 type sequence L description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 17) chain A residue 1027 type sequence D description BINDING SITE FOR RESIDUE ANP A 1201 source : AC1 18) chain A residue 880 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 982 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 887 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19105183 source Swiss-Prot : SWS_FT_FI6 21) chain A residue 1044 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:Q9M0G7, ECO:0000255 source Swiss-Prot : SWS_FT_FI10 22) chain A residue 1052 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:C0LGT6 source Swiss-Prot : SWS_FT_FI11 23) chain A residue 1072 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000255 source Swiss-Prot : SWS_FT_FI12 24) chain A residue 891 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 25) chain A residue 981 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 26) chain A residue 1035 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 27) chain A residue 1042 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 1060 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 29) chain A residue 956 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:19124768 source Swiss-Prot : SWS_FT_FI8 30) chain A residue 1039 type MOD_RES sequence X description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 31) chain A residue 1045 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 32) chain A residue 1049 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 33) chain A residue 889-912 type prosite sequence IGSGGFGDVYKAILKDGSAVAIKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGFGDVYkAilkdgsav..........AIKK source prosite : PS00107 34) chain A residue 1005-1017 type prosite sequence IIHRDXKSSNVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKssNVLL source prosite : PS00108 35) chain A 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 36) chain A residue 889 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 911 type BINDING sequence K description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 957 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 963 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 1009 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 1027 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 872 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:11027724, ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI4

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