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 | 60 |
Details | Zinc finger: {"description":"PHD-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 50 |
Details | Zinc finger: {"description":"PHD-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 15 |
Details | Region: {"description":"Interaction with HDGFL2","evidences":[{"source":"PubMed","id":"32459350","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"32459350","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"5-glutamyl serotonin; alternate","evidences":[{"source":"PubMed","id":"30867594","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"PubMed","id":"20228790","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Symmetric dimethylarginine; by PRMT5; alternate","evidences":[{"source":"UniProtKB","id":"P68433","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5","evidences":[{"source":"PubMed","id":"10464286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11856369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12560483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15681610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16457588","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by PKC and CHEK1","evidences":[{"source":"PubMed","id":"12560483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18066052","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18243098","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22901803","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |