3SMQ
Crystal structure of protein arginine methyltransferase 3
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TDU A 1 |
| Chain | Residue |
| A | GLY245 |
| A | THR466 |
| A | ALA467 |
| A | GLU248 |
| A | VAL387 |
| A | ASP389 |
| A | LYS392 |
| A | HIS393 |
| A | ARG396 |
| A | VAL420 |
| A | GLU422 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1000 |
| Chain | Residue |
| A | SER388 |
| A | SER463 |
| A | MET464 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"O70467","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in complex with SAH.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2FYT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
