3F2K
Structure of the transposase domain of human Histone-lysine N-methyltransferase SETMAR
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 227 |
| Chain | Residue |
| A | ASP38 |
| A | ASP130 |
| A | HOH241 |
| A | HOH242 |
| A | HOH259 |
| A | HOH469 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 227 |
| Chain | Residue |
| B | HOH259 |
| B | HOH260 |
| B | HOH331 |
| B | ASP38 |
| B | ASP130 |
| B | HOH230 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ALA51 | |
| A | LYS143 | |
| B | ALA51 | |
| B | LYS143 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:18790802 |
| Chain | Residue | Details |
| A | TRP53 | |
| B | TRP53 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CHEK1 => ECO:0000269|PubMed:22231448, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PHE63 | |
| B | PHE63 |
