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 | 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 | 0018364 | biological_process | peptidyl-glutamine methylation |
A | 0032259 | biological_process | methylation |
A | 0036009 | molecular_function | protein-glutamine N-methyltransferase activity |
A | 0043414 | biological_process | macromolecule methylation |
A | 0102559 | molecular_function | protein-(glutamine-N5) methyltransferase activity |
B | 0003676 | molecular_function | nucleic acid binding |
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 | 0018364 | biological_process | peptidyl-glutamine methylation |
B | 0032259 | biological_process | methylation |
B | 0036009 | molecular_function | protein-glutamine N-methyltransferase activity |
B | 0043414 | biological_process | macromolecule methylation |
B | 0102559 | molecular_function | protein-(glutamine-N5) 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 | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY129 | |
B | GLY129 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18247349, ECO:0000269|Ref.5 |
Chain | Residue | Details |
A | ASP151 | |
A | PHE180 | |
A | ASN197 | |
B | ASP151 | |
B | PHE180 | |
B | ASN197 |
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 | PHE100 | electrostatic stabiliser |
A | ASN197 | electrostatic stabiliser |
A | PRO198 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 703 |
Chain | Residue | Details |
B | PHE100 | electrostatic stabiliser |
B | ASN197 | electrostatic stabiliser |
B | PRO198 | electrostatic stabiliser |