2FYT
Human HMT1 hnRNP methyltransferase-like 3 (S. cerevisiae) protein
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH A 549 |
| Chain | Residue |
| A | TYR241 |
| A | GLN303 |
| A | SER304 |
| A | GLY328 |
| A | LYS329 |
| A | ILE330 |
| A | GLU331 |
| A | GLU346 |
| A | MET357 |
| A | SER360 |
| A | HOH550 |
| A | HIS247 |
| A | HOH552 |
| A | HOH562 |
| A | HOH582 |
| A | MET250 |
| A | ARG256 |
| A | GLY280 |
| A | CYS281 |
| A | ILE285 |
| A | LEU286 |
| A | ASP302 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1or8 |
| Chain | Residue | Details |
| A | GLU355 | |
| A | GLU346 |
