5SZC
Structure of human Dpf3 double-PHD domain bound to histone H3 tail peptide with monomethylated K4 and acetylated K14
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | CYS262 |
A | CYS265 |
A | HIS292 |
A | CYS295 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | CYS284 |
A | CYS287 |
A | CYS313 |
A | CYS316 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN A 403 |
Chain | Residue |
A | CYS322 |
A | HIS342 |
A | CYS345 |
A | CYS319 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN A 404 |
Chain | Residue |
A | CYS334 |
A | CYS337 |
A | CYS360 |
A | CYS363 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue MPD A 405 |
Chain | Residue |
A | TYR261 |
A | LEU266 |
A | ARG277 |
A | PRO278 |
A | TRP364 |
A | HOH508 |
A | HOH576 |
Functional Information from PROSITE/UniProt
site_id | PS01359 |
Number of Residues | 80 |
Details | ZF_PHD_1 Zinc finger PHD-type signature. CadCgrsghptclqftlnmteavktykwqcieckscilcgtsenddql.LfCdd..Cdrg.YHmyClnppvaeppegs.................................WsChlC |
Chain | Residue | Details |
A | CYS284-CYS363 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635 |
Chain | Residue | Details |
H | ARG2 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 |
Chain | Residue | Details |
H | THR3 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
H | MLZ4 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 |
Chain | Residue | Details |
H | GLN5 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 |
Chain | Residue | Details |
H | THR6 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 |
Chain | Residue | Details |
H | ARG8 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
H | LYS9 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: 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 |
Chain | Residue | Details |
H | SER10 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 |
Chain | Residue | Details |
H | THR11 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
H | ALY14 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635 |
Chain | Residue | Details |
H | ARG17 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
H | LYS18 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | LIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806 |
Chain | Residue | Details |
H | LYS18 |