Research workbench
Covalent ternary structure of hhai methyltransferase, DNA and S- adenosyl-L-homocysteine
Analyse Covalent ternary structure of hhai methyltransferase, DNA and S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MHT
- Type
- protein + DNA
- Length
- 352 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(P*GP*AP*TP*AP*GP*(C36)P*GP*CP*TP*AP*TP*C)-3'); DNA…
- EC
- 2.1.1.73
- UniProt
- P05102
- Ligands
- SAH
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | DNA (5'-D(P*GP*AP*TP*AP*GP*(C36)P*GP*CP*TP*AP*TP*C)-3') | dna | 12 | — | — |
| C | DNA (5'-D(*TP*GP*AP*TP*AP*GP*(C36)P*GP*CP*TP*AP*TP*C)-3') | dna | 13 | — | — |
| A | Protein (hhai methyltransferase) (EC 2.1.1.73) | protein | 327 | 32% helix, 20% strand | P05102 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains C, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.73 | 0.87 | 35 | SAH |
| 2 | 57 | 0.73 | 0.99 | 19 | empty |
| 3 | 151 | 0.57 | 0.83 | 18 | empty |
| 4 | 108 | 0.43 | 0.78 | 14 | empty |
| 5 | 59 | 0.39 | 0.80 | 16 | empty |
Interfaces
3 interfaces between chains.
- C–A · 1030 Ų buried · 39 hydrogen bonds · protein-nucleic
- B–A · 727 Ų buried · 11 hydrogen bonds · protein-nucleic
- B–C · 548 Ų buried · 43 hydrogen bonds · nucleic-nucleic
Modifications
Observed in the structure: 2 modified (nucleotide modification).
Compared structures
- 1MHT · Covalent ternary structure of hhai methyltransferase, DNA and S-adenosyl-L-homocysteine · the same entry in another collection · chain B against B, TM-score 1.00
- P05102 · AlphaFold monomer V2.0 prediction for modification methylase hhai (P05102) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P05102
- Elsewhere: RCSB PDB 1MHT · PDBe 1MHT · UniProt P05102
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