eF-site ID 4q5j-ABEF PDB Code 4q5j Chain A, B, E, F 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 B:  DLEVLFQGPHXPLRKLTFADLLQATNGFHNDSLIGSGGFG DVYKAILKDGSAVAIKKLIHDREFXAEXETIGKIKHRNLV PLLGYCKVGDERLLVYEFXKYGSLEDVLHVKLNWSTRRKI AIGSARGLAFLHHNCSPHIIHRDXKSSNVLLDENLEARVS DFGXARLXSAXDXHLXVXTLAGTPGYVPPEYYQXFRCSTK GDVYSYGVVLLELLTGKRPTDSPDFGDNNLVGWVKQHAKL RISDVFDPELXKEDPALEIELLQHLKVAVACLDDRAWRRP TXVQVXAXFKEIQA E:  MEELQAAIQAAIAHC F:  TMEELQAAIQAAIAHC 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 B residue 892 type sequence G description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 19) chain B residue 893 type sequence G description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 20) chain B residue 897 type sequence V description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 21) chain B residue 909 type sequence A description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 22) chain B residue 911 type sequence K description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 23) chain B residue 957 type sequence E description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 24) chain B residue 959 type sequence X description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 25) chain B residue 962 type sequence G description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 26) chain B residue 963 type sequence S description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 27) chain B residue 966 type sequence D description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 28) chain B residue 1011 type sequence K description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 29) chain B residue 1013 type sequence S description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 30) chain B residue 1014 type sequence N description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 31) chain B residue 1016 type sequence L description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 32) chain B residue 1027 type sequence D description BINDING SITE FOR RESIDUE ANP B 1201 source : AC2 33) chain A residue 880 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 982 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 880 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 36) chain B residue 982 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:15894717 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 887 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19105183 source Swiss-Prot : SWS_FT_FI6 38) chain B residue 887 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19105183 source Swiss-Prot : SWS_FT_FI6 39) chain A residue 1044 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:Q9M0G7, ECO:0000255 source Swiss-Prot : SWS_FT_FI10 40) chain B residue 1044 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:Q9M0G7, ECO:0000255 source Swiss-Prot : SWS_FT_FI10 41) chain A residue 1052 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:C0LGT6 source Swiss-Prot : SWS_FT_FI11 42) chain B residue 1052 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:C0LGT6 source Swiss-Prot : SWS_FT_FI11 43) chain A residue 1072 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000255 source Swiss-Prot : SWS_FT_FI12 44) chain B residue 1072 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000255 source Swiss-Prot : SWS_FT_FI12 45) chain A residue 891 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 46) chain B residue 1035 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 47) chain B residue 1042 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 48) chain B residue 1060 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 49) chain A residue 981 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 50) chain A residue 1035 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 51) chain A residue 1042 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 52) chain A residue 1060 type MOD_RES sequence X description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 53) chain B residue 891 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 54) chain B residue 981 type MOD_RES sequence S description Phosphoserine => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 55) chain A residue 956 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:19124768 source Swiss-Prot : SWS_FT_FI8 56) chain B residue 956 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:19124768 source Swiss-Prot : SWS_FT_FI8 57) chain A residue 1039 type MOD_RES sequence X description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 58) chain A residue 1045 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 59) chain A residue 1049 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 60) chain B residue 1039 type MOD_RES sequence X description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 61) chain B residue 1045 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 62) chain B residue 1049 type MOD_RES sequence T description Phosphothreonine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 63) chain A residue 889-912 type prosite sequence IGSGGFGDVYKAILKDGSAVAIKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGFGDVYkAilkdgsav..........AIKK source prosite : PS00107 64) chain A residue 1005-1017 type prosite sequence IIHRDXKSSNVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKssNVLL source prosite : PS00108 65) 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 66) 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 67) chain A residue 889 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 889 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 911 type BINDING sequence K description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 70) chain B residue 1027 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 71) chain A residue 957 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 72) chain A residue 963 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 73) chain A residue 1009 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 74) chain A residue 1027 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 911 type BINDING sequence K description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 957 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 77) chain B residue 963 type BINDING sequence S description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 78) chain B residue 1009 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24461462 source Swiss-Prot : SWS_FT_FI3 79) 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 80) 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

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