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Crystal structure of the Q7VLF5_HAEDU protein from haemophilus ducreyi. northeast structural genomics consortium target HDR25
Analyse Crystal structure of the Q7VLF5_HAEDU protein from haemophilus ducreyi.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UN9
- Type
- protein
- Length
- 269 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q7VLF5
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 69 | 72% helix, 0% strand | Q7VLF5 |
| B | Uncharacterized protein | protein | 65 | 72% helix, 0% strand | Q7VLF5 |
| C | Uncharacterized protein | protein | 68 | 72% helix, 0% strand | Q7VLF5 |
| D | Uncharacterized protein | protein | 67 | 81% helix, 0% strand | Q7VLF5 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.51 | 0.86 | 15 | empty |
| 2 | 136 | 0.48 | 0.78 | 24 | empty |
Interfaces
6 interfaces between chains.
- A–C · 1127 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 1021 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 911 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 860 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 841 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 6UN9 · Crystal Structure of the Q7VLF5_HAEDU protein from Haemophilus ducreyi. Northeast… · 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 Q7VLF5
- Elsewhere: RCSB PDB 6UN9 · PDBe 6UN9 · UniProt Q7VLF5
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