Research workbench
Crystal structure of rsmd methyltransferase of M. tuberculosis in complex with sinefungin reveals key interactions
Analyse Crystal structure of rsmd methyltransferase of M. tuberculosis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M1C
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible methyltransferase (methylase)
- UniProt
- I6XFS7
- Ligands
- SFG
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Possible methyltransferase (methylase) | protein | 184 | 30% helix, 23% strand | I6XFS7 |
Ligands and binding sites
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 | 251 | 0.61 | 0.80 | 38 | SFG, ACT |
Compared structures
- 6M1C · Crystal structure of RsmD methyltransferase of M. tuberculosis in complex with sinefungin… · 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 I6XFS7
- Elsewhere: RCSB PDB 6M1C · PDBe 6M1C · UniProt I6XFS7
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