2NQ5
Crystal structure of methyltransferase from Streptococcus mutans
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003871 | molecular_function | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0032259 | biological_process | methylation |
A | 0046872 | molecular_function | metal ion binding |
A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P82610 |
Chain | Residue | Details |
A | HIS683 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P82610 |
Chain | Residue | Details |
A | LYS19 | |
A | ASN115 | |
A | ILE420 | |
A | GLU473 | |
A | ASP478 | |
A | TYR501 | |
A | ARG504 | |
A | TRP550 | |
A | ASP588 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000269|PubMed:21840320, ECO:0007744|PDB:3T0C |
Chain | Residue | Details |
A | HIS630 | |
A | CYS632 | |
A | CYS715 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21840320, ECO:0007744|PDB:3T0C |
Chain | Residue | Details |
A | GLU654 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1uro |
Chain | Residue | Details |
A | GLU475 | |
A | TRP550 |