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Crystal structure of the M. tuberculosis O6-methylguanine methyltransferase R37L variant
Analyse Crystal structure of the M. tuberculosis O6-methylguanine methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BHC
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylated-DNA--protein-cysteine methyltransferase
- EC
- 2.1.1.63
- UniProt
- P0A696
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) | protein | 165 | 38% helix, 13% strand | P0A696 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.47 | 0.76 | 29 | empty |
| 2 | 58 | 0.30 | 0.75 | 14 | empty |
Compared structures
- 4BHC · Crystal structure of the M. tuberculosis O6-methylguanine methyltransferase R37L variant · 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 P0A696
- Elsewhere: RCSB PDB 4BHC · PDBe 4BHC · UniProt P0A696
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