Research workbench
Mycobacterium tuberculosis protein RV1155 in complex with co-enzyme F420
Analyse Mycobacterium tuberculosis protein RV1155 in complex with co-enzyme F420 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QVB
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RV1155 protein
- UniProt
- L0NRR9
- Ligands
- F42, NA
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RV1155 protein | protein | 141 | 31% helix, 39% strand | L0NRR9 |
| B | RV1155 protein | protein | 144 | 30% helix, 36% strand | L0NRR9 |
Ligands and binding sites
- F42 · Coenzyme F420 · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · chains B
- FMT · Formic acid · additive · 5 copies · chains A, B
- PDO · 1,3-propandiol · additive · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- PGO · S-1,2-propanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 335 | 0.59 | 0.76 | 36 | F42 |
| 2 | 179 | 0.46 | 0.75 | 30 | F42 |
| 3 | 73 | 0.38 | 0.78 | 20 | EDO |
Interfaces
1 interface between chains.
- A–B · 1259 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4QVB · Mycobacterium tuberculosis protein Rv1155 in complex with co-enzyme F420 · 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 L0NRR9
- Elsewhere: RCSB PDB 4QVB · PDBe 4QVB · UniProt L0NRR9
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