MolNFT v1 · #9152 · protein
Crystal structure of the hhai DNA methyltransferase complexed with S- adenosyl-L-methionine
1HMY · Haeiii methyltransferase: “Crystal structure of the hhai DNA methyltransferase complexed with S- adenosyl-L-methionine”. X-ray diffraction, 1 ligand (SAM), 2 pockets (best druggability 0.67). MolNFT v1 #9152 on GenesisL1: 3D…
- PDB
- 1HMY
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Haeiii methyltransferase
- EC
- 2.1.1.37
- UniProt
- P05102
- Ligands
- SAM
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Haeiii methyltransferase (EC 2.1.1.37) | protein | 327 | 29% helix, 18% strand | P05102 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.67 | 0.82 | 35 | SAM |
| 2 | 61 | 0.32 | 0.76 | 18 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1HMY · Crystal structure of the hhai DNA methyltransferase complexed with S-adenosyl-L-methionine · the same entry in another collection · chain A against A, 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 0.95
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 1HMY · PDBe 1HMY · UniProt P05102
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