1SG9
Crystal structure of Thermotoga maritima protein HEMK, an N5-glutamine methyltransferase
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 | 0032259 | biological_process | methylation |
| A | 0036009 | molecular_function | protein-glutamine N-methyltransferase activity |
| 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 | 0032259 | biological_process | methylation |
| B | 0036009 | molecular_function | protein-glutamine N-methyltransferase activity |
| B | 0102559 | molecular_function | protein-(glutamine-N5) methyltransferase activity |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0006479 | biological_process | protein methylation |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008170 | molecular_function | N-methyltransferase activity |
| C | 0008276 | molecular_function | protein methyltransferase activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0036009 | molecular_function | protein-glutamine N-methyltransferase activity |
| C | 0102559 | molecular_function | protein-(glutamine-N5) methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAM A 301 |
| Chain | Residue |
| A | PHE100 |
| A | GLU179 |
| A | PHE180 |
| A | ASN197 |
| A | GLU217 |
| A | ALA218 |
| A | GLN400 |
| A | HOH401 |
| A | HOH404 |
| A | HOH405 |
| A | HOH415 |
| A | PRO102 |
| A | HOH421 |
| A | HOH444 |
| A | THR106 |
| A | ILE128 |
| A | GLY129 |
| A | THR130 |
| A | ILE135 |
| A | ASP151 |
| A | VAL152 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAM B 302 |
| Chain | Residue |
| B | PHE100 |
| B | PRO102 |
| B | THR106 |
| B | GLY129 |
| B | THR130 |
| B | ILE135 |
| B | ASP151 |
| B | VAL152 |
| B | GLU179 |
| B | PHE180 |
| B | ASN197 |
| B | GLU217 |
| B | ALA218 |
| B | GLN401 |
| B | HOH405 |
| B | HOH406 |
| B | HOH408 |
| B | HOH420 |
| B | HOH468 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAM C 303 |
| Chain | Residue |
| C | PHE100 |
| C | PRO102 |
| C | GLY129 |
| C | THR130 |
| C | GLY131 |
| C | ALA134 |
| C | ASP151 |
| C | GLU179 |
| C | PHE180 |
| C | ASN197 |
| C | GLU217 |
| C | ALA218 |
| C | GLN402 |
| C | HOH405 |
| C | HOH407 |
| C | HOH408 |
| C | HOH410 |
| C | HOH413 |
| C | HOH414 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GLN A 400 |
| Chain | Residue |
| A | PHE100 |
| A | ARG103 |
| A | ASN197 |
| A | PRO198 |
| A | TYR200 |
| A | SAM301 |
| A | HOH496 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLN B 401 |
| Chain | Residue |
| B | PHE100 |
| B | ARG103 |
| B | ASN197 |
| B | PRO198 |
| B | TYR200 |
| B | GLU246 |
| B | SAM302 |
| B | HOH416 |
| B | HOH477 |
| B | HOH478 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GLN C 402 |
| Chain | Residue |
| C | PHE100 |
| C | ARG103 |
| C | ASN197 |
| C | PRO198 |
| C | TYR200 |
| C | SAM303 |
| C | HOH416 |
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 | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY129 | |
| B | GLY129 | |
| C | GLY129 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| 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 | |
| C | ASP151 | |
| C | PHE180 | |
| C | ASN197 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qam |
| Chain | Residue | Details |
| A | ASP151 | |
| A | ASN197 | |
| A | GLY129 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qam |
| Chain | Residue | Details |
| B | ASP151 | |
| B | ASN197 | |
| B | GLY129 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qam |
| Chain | Residue | Details |
| C | ASP151 | |
| C | ASN197 | |
| C | GLY129 |
| 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 |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 703 |
| Chain | Residue | Details |
| C | PHE100 | electrostatic stabiliser |
| C | ASN197 | electrostatic stabiliser |
| C | PRO198 | electrostatic stabiliser |
