eF-site ID 5fb0-ACDF PDB Code 5fb0 Chain A, C, D, F click to enlarge Title Crystal Structure of a PHD finger bound to histone H3 T3ph peptide Classification TRANSCRIPTION/STRUCTURAL PROTEIN Compound Nuclear autoantigen Sp-100 Source Homo sapiens (Human) (K7EMV3_HUMAN) Sequence A:  SDPCPENSNICEVCNKWGRLFCCDTCPRSFHEHCHIPSVE ANKNPWSCIFCRIKTIQERSGHQESEVLMRQMQPEEQLKC EFLLLKVYCDSKSSFFASEPYYGPQKPMWLNKVKTSLNEQ MYTRVEGFVQDMRLIFHNHKEFYREDKFTRLGIQVQDIFE KNFRNIFAIQET C:  SDPCPENSNICEVCNKWGRLFCCDTCPRSFHEHCHIPSVE ANKNPWSCIFCRIKTIQERSSGHQESEVLMRQMQPEEQLK CEFLLLKVYCDSKSSFFASEPGPQKPMWLNKVKTSLNEQM YTRVEGFVQDMRLIFHNHKEFYREDKFTRLGIQVQDIFEK NFRNIFAIQE D:  ARXKQTARKS F:  ARXKQTARKS Description (1)  Nuclear autoantigen Sp-100, Peptide from Histone H3 Functional site 1) chain A residue 705 type sequence C description binding site for residue ZN A 901 source : AC1 2) chain A residue 708 type sequence C description binding site for residue ZN A 901 source : AC1 3) chain A residue 725 type sequence H description binding site for residue ZN A 901 source : AC1 4) chain A residue 728 type sequence C description binding site for residue ZN A 901 source : AC1 5) chain A residue 717 type sequence C description binding site for residue ZN A 902 source : AC2 6) chain A residue 719 type sequence T description binding site for residue ZN A 902 source : AC2 7) chain A residue 720 type sequence C description binding site for residue ZN A 902 source : AC2 8) chain A residue 742 type sequence C description binding site for residue ZN A 902 source : AC2 9) chain A residue 745 type sequence C description binding site for residue ZN A 902 source : AC2 10) chain C residue 705 type sequence C description binding site for residue ZN C 901 source : AC3 11) chain C residue 708 type sequence C description binding site for residue ZN C 901 source : AC3 12) chain C residue 725 type sequence H description binding site for residue ZN C 901 source : AC3 13) chain C residue 728 type sequence C description binding site for residue ZN C 901 source : AC3 14) chain C residue 717 type sequence C description binding site for residue ZN C 902 source : AC4 15) chain C residue 719 type sequence T description binding site for residue ZN C 902 source : AC4 16) chain C residue 720 type sequence C description binding site for residue ZN C 902 source : AC4 17) chain C residue 742 type sequence C description binding site for residue ZN C 902 source : AC4 18) chain C residue 745 type sequence C description binding site for residue ZN C 902 source : AC4 19) chain D residue 2 type MOD_RES sequence R description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 20) chain F residue 2 type MOD_RES sequence R description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 21) chain D residue 3 type MOD_RES sequence X description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 22) chain F residue 3 type MOD_RES sequence X description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 23) chain D residue 4 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3 24) chain F residue 4 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3 25) chain D residue 5 type MOD_RES sequence Q description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 source Swiss-Prot : SWS_FT_FI4 26) chain F residue 5 type MOD_RES sequence Q description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 source Swiss-Prot : SWS_FT_FI4 27) chain D residue 6 type MOD_RES sequence T description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 source Swiss-Prot : SWS_FT_FI5 28) chain F residue 6 type MOD_RES sequence T description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 705-745 type prosite sequence CEVCNKWGRLFCCDTCPRSFHEHCHIPSVEANKNPWSCIF C description ZF_PHD_1 Zinc finger PHD-type signature. CevCnkwgrl.......................................FcCdt..Cprs.FHehChipsveanknp..................................WsCifC source prosite : PS01359 30) chain D residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI6 31) chain F residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI6 32) chain D residue 9 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI7 33) chain F residue 9 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI7 34) chain D residue 10 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 source Swiss-Prot : SWS_FT_FI8 35) chain F residue 10 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 source Swiss-Prot : SWS_FT_FI8

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