eF-site ID 5znp-ABPQ PDB Code 5znp Chain A, B, P, Q click to enlarge Title Crystal structure of PtSHL in complex with an H3K4me3 peptide Classification GENE REGULATION Compound SHORT LIFE family protein Source (H32_ARATH) Sequence A:  KAKAPRRTLDSYTVKPINKTVKPGDCVLMRPSDPSKPSYV AKIERIESDGRGPNVRVRVRWYYRPEESIGGRRQFHGSKE VFLSDHYDTQSADTIEGKCMVHSFKNYTKLDAVGNDDFFC RFEYNSSTGAFNPDRVAVYCKCEMPYNPDDLMVQCEGCSD WFHPACIEMSAEEAKRLDHFFCENC B:  AKAKAPRRTLDSYTVKPINKTVKPGDCVLMRPSDPSKPSY VAKIERIESDGRGPNVRVRVRWYYRPEESIGGRRQFHGSK EVFLSDHYDTQSADTIEGKCMVHSFKNYTKLDAVGNDDFF CRFEYNSSTGAFNPDRVAVYCKCEMPYNPDDLMVQCEGCS DWFHPACIEMSAEEAKRLDHFFCENC P:  TXQTARKS Q:  ARTXQTARK Description Functional site 1) chain A residue 142 type sequence C description binding site for residue ZN A 501 source : AC1 2) chain A residue 144 type sequence C description binding site for residue ZN A 501 source : AC1 3) chain A residue 165 type sequence H description binding site for residue ZN A 501 source : AC1 4) chain A residue 168 type sequence C description binding site for residue ZN A 501 source : AC1 5) chain A residue 157 type sequence C description binding site for residue ZN A 502 source : AC2 6) chain A residue 160 type sequence C description binding site for residue ZN A 502 source : AC2 7) chain A residue 184 type sequence C description binding site for residue ZN A 502 source : AC2 8) chain A residue 187 type sequence C description binding site for residue ZN A 502 source : AC2 9) chain B residue 142 type sequence C description binding site for residue ZN B 501 source : AC3 10) chain B residue 144 type sequence C description binding site for residue ZN B 501 source : AC3 11) chain B residue 165 type sequence H description binding site for residue ZN B 501 source : AC3 12) chain B residue 168 type sequence C description binding site for residue ZN B 501 source : AC3 13) chain B residue 157 type sequence C description binding site for residue ZN B 502 source : AC4 14) chain B residue 160 type sequence C description binding site for residue ZN B 502 source : AC4 15) chain B residue 184 type sequence C description binding site for residue ZN B 502 source : AC4 16) chain B residue 187 type sequence C description binding site for residue ZN B 502 source : AC4 17) chain P residue 10 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 142-157 type prosite sequence CKCEMPYNPDDLMVQC description EGF_2 EGF-like domain signature 2. CkCemPYnpddlmvqC source prosite : PS01186 19) chain A residue 142-187 type prosite sequence CKCEMPYNPDDLMVQCEGCSDWFHPACIEMSAEEAKRLDH FFCENC description ZF_PHD_1 Zinc finger PHD-type signature. Ck.Cempynpddlm...................................VqCeg..Csdw.FHpaCiemsaeeakrldh................................FfCenC source prosite : PS01359 20) 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_FI2 21) chain Q 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_FI2 22) chain P residue 9 type MOD_RES sequence K 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_FI3 23) chain Q residue 9 type MOD_RES sequence K 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_FI3

Display surface Download Links