MolNFT v1 · #108156 · protein
Crystal structure of histidine bound histidine-specific methyltransferase egtd from mycobacterium smegmatis
4UY7: “Crystal structure of histidine bound histidine-specific methyltransferase egtd from mycobacterium smegmatis”. X-ray diffraction, 1 ligand (HIS), 4 pockets (best druggability 0.75). MolNFT v1 #108156 on GenesisL1: 3D structure…
- PDB
- 4UY7
- Type
- protein
- Length
- 653 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine-specific methyltransferase egtd
- EC
- 2.1.1.44
- UniProt
- A0R5M8
- Ligands
- HIS
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine-specific methyltransferase egtd (EC 2.1.1.44) | protein | 327 | 43% helix, 27% strand | A0R5M8 |
| B | Histidine-specific methyltransferase egtd (EC 2.1.1.44) | protein | 326 | 40% helix, 26% strand | A0R5M8 |
Ligands and binding sites
- HIS · Histidine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 886 | 0.75 | 0.79 | 78 | HIS |
| 2 | 796 | 0.74 | 0.79 | 78 | HIS |
| 3 | 105 | 0.47 | 0.80 | 22 | empty |
| 4 | 125 | 0.46 | 0.78 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 737 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4UY7 · Crystal structure of Histidine bound Histidine-specific methyltransferase EgtD from… · 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 B 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 4UY7 · PDBe 4UY7 · UniProt A0R5M8
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