5Y20
Crystal structure of AL1 PHD finger bound to H3K4me3
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 101 |
| Chain | Residue |
| A | CYS7 |
| A | CYS10 |
| A | HIS31 |
| A | CYS34 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 102 |
| Chain | Residue |
| A | CYS23 |
| A | CYS26 |
| A | CYS50 |
| A | CYS53 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3 |
| Chain | Residue |
| A | CYS10 |
| A | ASN13 |
| A | TYR14 |
| A | PHE19 |
| A | TRP20 |
| A | TRP29 |
| A | HOH213 |
| P | THR3 |
| P | THR6 |
| P | ALA7 |
| P | HOH101 |
| P | HOH104 |
| A | THR5 |
Functional Information from PROSITE/UniProt
| site_id | PS01359 |
| Number of Residues | 47 |
| Details | ZF_PHD_1 Zinc finger PHD-type signature. CgsCggnytndefw...................................IcCdv..Cerw.YHgkCvkitpakaesikq................................YkCpsC |
| Chain | Residue | Details |
| A | CYS7-CYS53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Site: {"description":"Histone H3K4me3 binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Citrulline; alternate","evidences":[{"source":"PubMed","id":"16567635","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by HASPIN and VRK1","evidences":[{"source":"PubMed","id":"15681610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31527692","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
