1BHJ
CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)
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 | 0006544 | biological_process | glycine metabolic process |
| A | 0006555 | biological_process | methionine metabolic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0016594 | molecular_function | glycine binding |
| A | 0017174 | molecular_function | glycine N-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0034708 | cellular_component | methyltransferase complex |
| 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 | 0098603 | molecular_function | selenol Se-methyltransferase activity |
| A | 1901052 | biological_process | sarcosine metabolic process |
| A | 1904047 | molecular_function | S-adenosyl-L-methionine 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 | 0006544 | biological_process | glycine metabolic process |
| B | 0006555 | biological_process | methionine metabolic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016594 | molecular_function | glycine binding |
| B | 0017174 | molecular_function | glycine N-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0034708 | cellular_component | methyltransferase complex |
| 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 | 0098603 | molecular_function | selenol Se-methyltransferase activity |
| B | 1901052 | biological_process | sarcosine metabolic process |
| B | 1904047 | molecular_function | S-adenosyl-L-methionine binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22037183, ECO:0000312|PDB:3THR, ECO:0000312|PDB:3THS |
| Chain | Residue | Details |
| A | VAL4 | |
| A | MET215 | |
| A | LEU240 | |
| B | VAL4 | |
| B | MET215 | |
| B | LEU240 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22037183, ECO:0000312|PDB:3THS |
| Chain | Residue | Details |
| A | ARG6 | |
| B | ARG6 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0007744|PDB:1NBH |
| Chain | Residue | Details |
| A | ALA22 | |
| B | ALA22 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI |
| Chain | Residue | Details |
| A | GLN31 | |
| A | THR41 | |
| A | ALA86 | |
| A | TRP117 | |
| B | GLN31 | |
| B | THR41 | |
| B | ALA86 | |
| B | TRP117 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8810903, ECO:0007744|PDB:1XVA |
| Chain | Residue | Details |
| A | ILE34 | |
| A | ASN176 | |
| A | THR221 | |
| B | ILE34 | |
| B | ASN176 | |
| B | THR221 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0000269|PubMed:8810903, ECO:0000312|PDB:1XVA, ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI |
| Chain | Residue | Details |
| A | CYS65 | |
| B | CYS65 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0000269|PubMed:8810903, ECO:0007744|PDB:1NBI, ECO:0007744|PDB:1XVA |
| Chain | Residue | Details |
| A | GLY137 | |
| B | GLY137 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylvaline => ECO:0000269|PubMed:2822402 |
| Chain | Residue | Details |
| A | ASP2 | |
| B | ASP2 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QXF8 |
| Chain | Residue | Details |
| A | LEU10 | |
| B | LEU10 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXF8 |
| Chain | Residue | Details |
| A | ILE34 | |
| B | ILE34 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXF8 |
| Chain | Residue | Details |
| A | ALA46 | |
| A | ASN191 | |
| A | SER196 | |
| A | ASP201 | |
| B | ALA46 | |
| B | ASN191 | |
| B | SER196 | |
| B | ASP201 |
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 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 23 |
| Chain | Residue | Details |
| A | ALA22 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | ASN138 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LEU143 | activator |
| A | ASN176 | electrostatic stabiliser |
| A | LYS195 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 23 |
| Chain | Residue | Details |
| B | ALA22 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ASN138 | electrostatic stabiliser, hydrogen bond acceptor |
| B | LEU143 | activator |
| B | ASN176 | electrostatic stabiliser |
| B | LYS195 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
