2AZT
Crystal structure of H176N mutant of human Glycine N-Methyltransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005542 | molecular_function | folic acid binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006111 | biological_process | regulation of gluconeogenesis |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016594 | molecular_function | glycine binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017174 | molecular_function | glycine N-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046498 | biological_process | S-adenosylhomocysteine metabolic process |
| A | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 1901052 | biological_process | sarcosine metabolic process |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005542 | molecular_function | folic acid binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006111 | biological_process | regulation of gluconeogenesis |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016594 | molecular_function | glycine binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017174 | molecular_function | glycine N-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046498 | biological_process | S-adenosylhomocysteine metabolic process |
| B | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 1901052 | biological_process | sarcosine metabolic process |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 3000 |
| Chain | Residue |
| B | GLN58 |
| B | PHE79 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME A 1188 |
| Chain | Residue |
| A | CYS187 |
| A | ALA188 |
| A | PRO189 |
| A | VAL204 |
| A | THR206 |
| A | ASN212 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 1285 |
| Chain | Residue |
| A | CYS284 |
| A | ILE282 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME B 2188 |
| Chain | Residue |
| B | ARG53 |
| B | GLN54 |
| B | GLY186 |
| B | CYS187 |
| B | PRO189 |
| B | VAL204 |
| B | THR206 |
| B | ASN212 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME B 2249 |
| Chain | Residue |
| B | LEU183 |
| B | CYS248 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME B 2285 |
| Chain | Residue |
| B | HIS181 |
| B | LYS192 |
| B | ILE282 |
| B | CYS284 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CIT A 1000 |
| Chain | Residue |
| A | TYR33 |
| A | GLY139 |
| A | ASN140 |
| A | HIS144 |
| A | ARG177 |
| A | ASN193 |
| A | TYR222 |
| A | TYR244 |
| A | TYR285 |
| B | GLU15 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CIT B 2000 |
| Chain | Residue |
| A | GLU15 |
| B | TYR33 |
| B | GLY139 |
| B | ASN140 |
| B | HIS144 |
| B | ASN193 |
| B | TYR222 |
| B | TYR244 |
| B | TYR285 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13255","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
