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 | 0006111 | biological_process | regulation of gluconeogenesis |
| A | 0006544 | biological_process | glycine metabolic process |
| A | 0006546 | biological_process | glycine catabolic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016594 | molecular_function | glycine binding |
| A | 0017174 | molecular_function | glycine N-methyltransferase activity |
| A | 0018013 | biological_process | N-terminal peptidyl-glycine methylation |
| A | 0034708 | cellular_component | methyltransferase complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| A | 0050843 | biological_process | S-adenosylmethionine catabolic process |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0098603 | molecular_function | selenol Se-methyltransferase activity |
| A | 1901052 | biological_process | obsolete sarcosine metabolic process |
| A | 1901605 | biological_process | alpha-amino acid 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 | 0006111 | biological_process | regulation of gluconeogenesis |
| B | 0006544 | biological_process | glycine metabolic process |
| B | 0006546 | biological_process | glycine catabolic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016594 | molecular_function | glycine binding |
| B | 0017174 | molecular_function | glycine N-methyltransferase activity |
| B | 0018013 | biological_process | N-terminal peptidyl-glycine methylation |
| B | 0034708 | cellular_component | methyltransferase complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046500 | biological_process | S-adenosylmethionine metabolic process |
| B | 0050843 | biological_process | S-adenosylmethionine catabolic process |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0098603 | molecular_function | selenol Se-methyltransferase activity |
| B | 1901052 | biological_process | obsolete sarcosine metabolic process |
| B | 1901605 | biological_process | alpha-amino acid 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 site: {"evidences":[{"source":"PubMed","id":"22037183","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THR","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3THS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22037183","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylvaline","evidences":[{"source":"PubMed","id":"2822402","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| 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 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 23 |
| Chain | Residue | Details |
| A | TYR21 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLY137 | electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS142 | activator |
| A | ARG175 | electrostatic stabiliser |
| A | TYR194 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 23 |
| Chain | Residue | Details |
| B | TYR21 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | GLY137 | electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS142 | activator |
| B | ARG175 | electrostatic stabiliser |
| B | TYR194 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
