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 | 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 | 0036211 | biological_process | protein modification process |
| 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 | 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 | 0036211 | biological_process | protein modification process |
| 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 | 28 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13255 |
| Chain | Residue | Details |
| A | SER3 | |
| A | LEU138 | |
| A | ARG177 | |
| A | HIS216 | |
| A | TYR222 | |
| A | ARG241 | |
| B | SER3 | |
| B | TYR5 | |
| B | TYR21 | |
| B | TRP30 | |
| B | TYR33 | |
| A | TYR5 | |
| B | ARG40 | |
| B | ALA64 | |
| B | ASP85 | |
| B | ASN116 | |
| B | LEU138 | |
| B | ARG177 | |
| B | HIS216 | |
| B | TYR222 | |
| B | ARG241 | |
| 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:0000250|UniProtKB:Q9QXF8 |
| Chain | Residue | Details |
| A | SER9 | |
| B | SER9 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXF8 |
| Chain | Residue | Details |
| A | TYR33 | |
| B | TYR33 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXF8 |
| Chain | Residue | Details |
| A | LYS45 | |
| A | LYS192 | |
| A | LYS197 | |
| A | LYS202 | |
| B | LYS45 | |
| B | LYS192 | |
| B | LYS197 | |
| B | LYS202 |
