1R74
Crystal Structure 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 | 6 |
Details | BINDING SITE FOR RESIDUE BME A 1187 |
Chain | Residue |
A | GLN54 |
A | GLY186 |
A | CYS187 |
A | VAL204 |
A | THR206 |
A | ASN212 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CIT A 1001 |
Chain | Residue |
A | HIS144 |
A | ASN193 |
A | TYR244 |
A | TYR285 |
B | GLU15 |
A | TYR33 |
A | GLY139 |
A | ASN140 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BME B 2187 |
Chain | Residue |
B | ARG53 |
B | GLN54 |
B | GLY56 |
B | GLY186 |
B | CYS187 |
B | VAL204 |
B | THR206 |
B | ASN212 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME B 2264 |
Chain | Residue |
B | GLN257 |
B | CYS264 |
B | GLN265 |
B | HIS266 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME B 2284 |
Chain | Residue |
B | LYS192 |
B | CYS284 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT B 2001 |
Chain | Residue |
B | TYR33 |
B | GLY139 |
B | ASN140 |
B | HIS144 |
B | ASN193 |
B | TYR222 |
B | TYR244 |
B | TYR285 |
B | HOH2286 |
B | HOH2320 |
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 | VAL4 | |
A | GLY139 | |
A | ASN178 | |
A | MET217 | |
A | THR223 | |
A | LEU242 | |
B | VAL4 | |
B | ARG6 | |
B | ALA22 | |
B | GLN31 | |
B | ILE34 | |
A | ARG6 | |
B | THR41 | |
B | CYS65 | |
B | ALA86 | |
B | TRP117 | |
B | GLY139 | |
B | ASN178 | |
B | MET217 | |
B | THR223 | |
B | LEU242 | |
A | ALA22 | |
A | GLN31 | |
A | ILE34 | |
A | THR41 | |
A | CYS65 | |
A | ALA86 | |
A | TRP117 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P13255 |
Chain | Residue | Details |
A | ASP2 | |
B | ASP2 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QXF8 |
Chain | Residue | Details |
A | LEU10 | |
B | LEU10 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXF8 |
Chain | Residue | Details |
A | ILE34 | |
B | ILE34 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXF8 |
Chain | Residue | Details |
A | ALA46 | |
A | ASN193 | |
A | SER198 | |
A | ASP203 | |
B | ALA46 | |
B | ASN193 | |
B | SER198 | |
B | ASP203 |
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 |