6HPZ
Crystal structure of ENL (MLLT1) in complex with acetyllysine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 201 |
| Chain | Residue |
| A | VAL9 |
| A | ARG10 |
| A | CYS42 |
| A | ILE44 |
| A | PHE47 |
| A | ALA138 |
| A | GLY139 |
| A | HOH308 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 202 |
| Chain | Residue |
| A | ASP103 |
| A | PHE105 |
| A | ASP103 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue ALY A 203 |
| Chain | Residue |
| A | HIS56 |
| A | SER58 |
| A | PHE59 |
| A | GLY77 |
| A | TYR78 |
| A | ALA79 |
| A | GLY80 |
| A | HOH321 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Region: {"description":"Acylated histone binding","evidences":[{"source":"PubMed","id":"28241141","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5J9S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Site: {"description":"Acylated histone binding","evidences":[{"source":"PubMed","id":"28241141","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5J9S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
