eF-site ID 5yko-AP PDB Code 5yko Chain A, P click to enlarge Title Crystal structure of Arabidopsis thaliana JMJ14 catalytic domain in complex with NOG and H3K4me3 peptide Classification GENE REGULATION Compound Probable lysine-specific demethylase JMJ14 Source Arabidopsis thaliana (Mouse-ear cress) (H32_ARATH) Sequence A:  RWNPSEACRPLVDDAPIFYPTNEDFDDPLGYIEKLRSKAE SYGICRIVPPVAWRPPCPLKEKKIWENSKFPTRIQFIDLL QNRFGFQTGPDFTLAAFQKYDEYFKECYFQPKVKDLEGEY WRIVEQATDEVEVYYGADLETKKFGSGFPKYKPGYPISEA DQYSQCGWNLNNLSRLPGSVLAFESCDISGVIVPWLYVGM CFSTFCWHVEDHHLYSMNYLHTGDPKVWYGIPGNHAESFE NVMKKRLPDLFEEQPDLLHQLVTQLSPRILKEEGVPVYRA VQRSGEFILTFPKAYHSGFNCGFNCAEAVNVAPVDWLVHG QNAVEGYSKQRRKSSLSHDKLLLGAAMEATYCLWELSLSK KKTPVIARWKRVCSEDGLLTKAVKKRVQMEEERLNHLQDG FSLRKMEGDFDNKRERECFLCFYDLHMSASSCKCSPNRFA CLIHAKDLCSCESKDRYILIRHTLDELWALVRALEGDLDA IDLWASK P:  ARTXQTA Description Functional site 1) chain A residue 309 type sequence H description binding site for residue NI A 800 source : AC1 2) chain A residue 311 type sequence E description binding site for residue NI A 800 source : AC1 3) chain A residue 397 type sequence H description binding site for residue NI A 800 source : AC1 4) chain A residue 519 type sequence C description binding site for residue ZN A 801 source : AC2 5) chain A residue 522 type sequence C description binding site for residue ZN A 801 source : AC2 6) chain A residue 542 type sequence C description binding site for residue ZN A 801 source : AC2 7) chain A residue 545 type sequence H description binding site for residue ZN A 801 source : AC2 8) chain A residue 533 type sequence C description binding site for residue ZN A 802 source : AC3 9) chain A residue 535 type sequence C description binding site for residue ZN A 802 source : AC3 10) chain A residue 550 type sequence C description binding site for residue ZN A 802 source : AC3 11) chain A residue 552 type sequence C description binding site for residue ZN A 802 source : AC3 12) chain A residue 236 type sequence Y description binding site for residue OGA A 803 source : AC4 13) chain A residue 298 type sequence Y description binding site for residue OGA A 803 source : AC4 14) chain A residue 306 type sequence F description binding site for residue OGA A 803 source : AC4 15) chain A residue 309 type sequence H description binding site for residue OGA A 803 source : AC4 16) chain A residue 311 type sequence E description binding site for residue OGA A 803 source : AC4 17) chain A residue 317 type sequence S description binding site for residue OGA A 803 source : AC4 18) chain A residue 319 type sequence N description binding site for residue OGA A 803 source : AC4 19) chain A residue 327 type sequence K description binding site for residue OGA A 803 source : AC4 20) chain A residue 329 type sequence W description binding site for residue OGA A 803 source : AC4 21) chain A residue 397 type sequence H description binding site for residue OGA A 803 source : AC4 22) chain A residue 409 type sequence A description binding site for residue OGA A 803 source : AC4 23) chain P residue 4 type sequence X description binding site for residue OGA A 803 source : AC4 24) chain P residue 4 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16258034 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 311 type MOD_RES sequence E description N6-methyllysine; alternate => ECO:0000269|PubMed:12456661, ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15014946, ECO:0000269|PubMed:15598823 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 397 type MOD_RES sequence H description N6-methyllysine; alternate => ECO:0000269|PubMed:12456661, ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15014946, ECO:0000269|PubMed:15598823 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 522 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 533 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 535 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 542 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 545 type MOD_RES sequence H description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 550 type BINDING sequence C description BINDING => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI4 33) chain A residue 552 type BINDING sequence C description BINDING => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN source Swiss-Prot : SWS_FT_FI5 34) chain A residue 171 type SITE sequence F description Involved in histone H3A7 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI6 35) chain A residue 363 type SITE sequence V description Involved in histone H3A7 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI6 36) chain A residue 285 type SITE sequence E description Involved in histone H3R2 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI7 37) chain A residue 516 type SITE sequence E description Involved in histone H3R2 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI7 38) chain A residue 290 type SITE sequence S description Involved in histone H3K4me3 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI8 39) chain A residue 298 type SITE sequence Y description Involved in histone H3K4me3 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI8 40) chain A residue 312 type SITE sequence D description Involved in histone H3Q5 recognition => ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO source Swiss-Prot : SWS_FT_FI9

Display surface Download Links