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 |