Research workbench
Crystal structure of protein RV1636 from mycobacterium tuberculosis H37RV
Analyse Crystal structure of protein RV1636 from mycobacterium tuberculosis H37RV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TQ8
- Type
- protein
- Length
- 761 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein RV1636
- UniProt
- O06153
- Pockets
- 15 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F | Hypothetical protein RV1636 | protein | 127 | 40% helix, 24% strand | O06153 |
| E | Hypothetical protein RV1636 | protein | 126 | 41% helix, 22% strand | O06153 |
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 176 | 0.72 | 0.90 | 33 | empty |
| 2 | 186 | 0.72 | 0.89 | 36 | empty |
| 3 | 430 | 0.64 | 0.78 | 36 | empty |
| 4 | 444 | 0.64 | 0.77 | 41 | empty |
| 5 | 106 | 0.50 | 0.81 | 19 | empty |
Interfaces
8 interfaces between chains.
- C–D · 2146 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 2117 Ų buried · 34 hydrogen bonds · protein-protein
- E–F · 2101 Ų buried · 38 hydrogen bonds · protein-protein
- B–D · 1150 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 1133 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 1TQ8 · Crystal Structure of protein Rv1636 from Mycobacterium tuberculosis H37Rv · 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 O06153
- Elsewhere: RCSB PDB 1TQ8 · PDBe 1TQ8 · UniProt O06153
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