Research workbench
Bdellovibrio bacteriovorus dgcb fha domain, tail complex
Analyse Bdellovibrio bacteriovorus dgcb fha domain, tail complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HC0
- Type
- protein
- Length
- 420 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dgcb N-terminus; Ggdef domain protein
- UniProt
- Q6MPU8
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 4 distinct chains · 0% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dgcb N-terminus | protein | 7 | 0% helix, 0% strand | — |
| B | Ggdef domain protein | protein | 105 | 0% helix, 42% strand | Q6MPU8 |
| C, E | Ggdef domain protein | protein | 103 | 0% helix, 44% strand | Q6MPU8 |
| D | Ggdef domain protein | protein | 102 | 0% helix, 44% strand | Q6MPU8 |
Ligands and binding sites
- FMT · Formic acid · additive · chains C
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 | 895 | 0.69 | 0.74 | 102 | empty |
Interfaces
5 interfaces between chains.
- C–E · 392 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 389 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 266 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 257 Ų buried · 4 hydrogen bonds · protein-protein
- D–E · 245 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6HC0 · Bdellovibrio bacteriovorus DgcB FHA domain, tail complex · 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 Q6MPU8
- Elsewhere: RCSB PDB 6HC0 · PDBe 6HC0 · UniProt Q6MPU8
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