Research workbench
Crystal structure of histidine-specific methyltransferase egtd from mycobacterium smegmatis
Analyse Crystal structure of histidine-specific methyltransferase egtd from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UY5
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine-specific methyltransferase egtd
- EC
- 2.1.1.44
- UniProt
- A0R5M8
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine-specific methyltransferase egtd (EC 2.1.1.44) | protein | 326 | 42% helix, 27% strand | A0R5M8 |
Ligands and binding sites
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 | 724 | 0.73 | 0.79 | 78 | IMD, ACT |
| 2 | 60 | 0.50 | 0.86 | 15 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4UY5 · Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium… · the same entry in another collection · chain A against A, TM-score 1.00
- A0R5M8 · AlphaFold monomer V2.0 prediction for histidine N-alpha- methyltransferase (A0R5M8) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 A0R5M8
- Elsewhere: RCSB PDB 4UY5 · PDBe 4UY5 · UniProt A0R5M8
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