1R8X
Crystal Structure of Mouse Glycine N-Methyltransferase (Tetragonal Form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005542 | molecular_function | folic acid binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0006111 | biological_process | regulation of gluconeogenesis |
| A | 0006555 | biological_process | methionine metabolic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016594 | molecular_function | glycine binding |
| A | 0017174 | molecular_function | glycine N-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0005542 | molecular_function | folic acid binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005977 | biological_process | glycogen metabolic process |
| B | 0006111 | biological_process | regulation of gluconeogenesis |
| B | 0006555 | biological_process | methionine metabolic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016594 | molecular_function | glycine binding |
| B | 0017174 | molecular_function | glycine N-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| B | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 1146 |
| Chain | Residue |
| A | PRO144 |
| A | CYS146 |
| A | HIS214 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 1246 |
| Chain | Residue |
| A | ALA213 |
| A | CYS246 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS A 1247 |
| Chain | Residue |
| A | THR67 |
| A | ASP70 |
| A | LEU136 |
| A | SER139 |
| B | GLU15 |
| A | ASP62 |
| A | ALA64 |
| A | CYS65 |
| A | GLY66 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME B 2146 |
| Chain | Residue |
| B | CYS146 |
| B | HIS214 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME B 2262 |
| Chain | Residue |
| B | ARG255 |
| B | GLY260 |
| B | CYS262 |
| B | HIS264 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 2263 |
| Chain | Residue |
| A | GLU15 |
| B | ALA64 |
| B | CYS65 |
| B | GLY66 |
| B | THR67 |
| B | VAL69 |
| B | ASP70 |
| B | LEU136 |
| B | SER139 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13255 |
| Chain | Residue | Details |
| A | SER3 | |
| A | LEU136 | |
| A | ARG175 | |
| A | HIS214 | |
| A | TYR220 | |
| A | ARG239 | |
| B | SER3 | |
| B | TYR5 | |
| B | TYR21 | |
| B | TRP30 | |
| B | TYR33 | |
| A | TYR5 | |
| B | ARG40 | |
| B | ALA64 | |
| B | ASP85 | |
| B | ASN116 | |
| B | LEU136 | |
| B | ARG175 | |
| B | HIS214 | |
| B | TYR220 | |
| B | ARG239 | |
| A | TYR21 | |
| A | TRP30 | |
| A | TYR33 | |
| A | ARG40 | |
| A | ALA64 | |
| A | ASP85 | |
| A | ASN116 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P13255 |
| Chain | Residue | Details |
| A | VAL1 | |
| B | VAL1 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | SER9 | |
| B | SER9 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | TYR33 | |
| B | TYR33 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS45 | |
| A | LYS190 | |
| A | LYS195 | |
| A | LYS200 | |
| B | LYS45 | |
| B | LYS190 | |
| B | LYS195 | |
| B | LYS200 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xva |
| Chain | Residue | Details |
| A | GLU15 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xva |
| Chain | Residue | Details |
| B | GLU15 |
