1VQ1
Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0006415 | biological_process | translational termination |
| A | 0006479 | biological_process | protein methylation |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008170 | molecular_function | N-methyltransferase activity |
| A | 0008276 | molecular_function | protein methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0036009 | molecular_function | protein-glutamine N-methyltransferase activity |
| A | 0102559 | molecular_function | peptide chain release factor N(5)-glutamine methyltransferase activity |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0006415 | biological_process | translational termination |
| B | 0006479 | biological_process | protein methylation |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008170 | molecular_function | N-methyltransferase activity |
| B | 0008276 | molecular_function | protein methyltransferase activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0036009 | molecular_function | protein-glutamine N-methyltransferase activity |
| B | 0102559 | molecular_function | peptide chain release factor N(5)-glutamine methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAM A 301 |
| Chain | Residue |
| A | PHE100 |
| A | PHE180 |
| A | ASN197 |
| A | PRO198 |
| A | PRO199 |
| A | ALA218 |
| A | PHE228 |
| A | HOH303 |
| A | THR106 |
| A | GLY129 |
| A | THR130 |
| A | GLY131 |
| A | ASP151 |
| A | VAL152 |
| A | GLY178 |
| A | GLU179 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SAM B 301 |
| Chain | Residue |
| B | PHE100 |
| B | GLY129 |
| B | THR130 |
| B | GLY131 |
| B | ILE135 |
| B | ASP151 |
| B | VAL152 |
| B | GLU179 |
| B | PHE180 |
| B | ASN197 |
| B | PRO198 |
| B | PRO199 |
| B | GLU217 |
| B | ALA218 |
| B | PHE228 |
Functional Information from PROSITE/UniProt
| site_id | PS00092 |
| Number of Residues | 7 |
| Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. ILSNPPY |
| Chain | Residue | Details |
| A | ILE194-TYR200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18247349","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution.","authoringGroup":["Joint Center for Structural Genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details |
| Chain | Residue | Details |
| A | PHE100 | |
| A | PRO198 | |
| A | ASN197 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 703 |
| Chain | Residue | Details |
| A | LEU112 | electrostatic stabiliser |
| A | PHE213 | electrostatic stabiliser |
| A | GLU214 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 703 |
| Chain | Residue | Details |
| B | LEU112 | electrostatic stabiliser |
| B | PHE213 | electrostatic stabiliser |
| B | GLU214 | electrostatic stabiliser |
