3SOU
Structure of UHRF1 PHD finger in complex with histone H3 1-9 peptide
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | CYS315 |
A | CYS318 |
A | CYS326 |
A | CYS329 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 2 |
Chain | Residue |
A | CYS331 |
A | CYS334 |
A | HIS354 |
A | CYS357 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 3 |
Chain | Residue |
A | CYS349 |
A | CYS373 |
A | CYS376 |
A | CYS346 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 7 |
Chain | Residue |
A | HIS332 |
A | GLU375 |
B | HOH101 |
B | HIS317 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 4 |
Chain | Residue |
B | CYS331 |
B | CYS334 |
B | HIS354 |
B | CYS357 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 5 |
Chain | Residue |
B | CYS315 |
B | CYS318 |
B | CYS326 |
B | CYS329 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 6 |
Chain | Residue |
B | CYS346 |
B | CYS349 |
B | CYS373 |
B | CYS376 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 8 |
Chain | Residue |
A | HIS317 |
B | HOH102 |
B | HIS332 |
B | GLU375 |
Functional Information from PROSITE/UniProt
site_id | PS01359 |
Number of Residues | 62 |
Details | ZF_PHD_1 Zinc finger PHD-type signature. CkhCkddvnrlcrvcachlcggrqdpdkq....................LmCde..Cdma.FHiyCldpplssvpsede................................WyCpeC |
Chain | Residue | Details |
A | CYS315-CYS376 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635 |
Chain | Residue | Details |
D | ARG2 | |
E | ARG2 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 |
Chain | Residue | Details |
D | THR3 | |
E | THR3 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
D | LYS4 | |
E | LYS4 | |
B | PRO340 | |
B | GLN343 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 |
Chain | Residue | Details |
D | GLN5 | |
E | GLN5 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 |
Chain | Residue | Details |
D | THR6 | |
E | THR6 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 |
Chain | Residue | Details |
D | ARG8 | |
E | ARG8 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
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 |
D | LYS9 | |
E | LYS9 |