Research workbench
RV2966C of M. tuberculosis is a rsmd-like methyltransferase
Analyse RV2966C of M. tuberculosis is a rsmd-like methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P9N
- Type
- protein
- Length
- 182 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible methyltransferase (methylase)
- EC
- 2.1.1.-
- UniProt
- P95128
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Possible methyltransferase (methylase) (EC 2.1.1.-) | protein | 182 | 31% helix, 26% strand | P95128 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.62 | 0.79 | 38 | empty |
Compared structures
- 3P9N · Rv2966c of M. tuberculosis is a RsmD-like methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
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 P95128
- Elsewhere: RCSB PDB 3P9N · PDBe 3P9N · UniProt P95128
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