MolNFT v1 · #86810 · protein
Crystal structure of bsla - a bacterial hydrophobin
4BHU · Uncharacterized protein yuab: “Crystal structure of bsla - a bacterial hydrophobin”. X-ray diffraction, 1 ligand (CL), 12 pockets (best druggability 0.85). MolNFT v1 #86810 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4BHU
- Type
- protein
- Length
- 1,269 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein yuab
- UniProt
- P71014
- Ligands
- CL
- Pockets
- 12 · best druggability 0.85
Structure
x-ray diffraction · 5 distinct chains · 3% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G, H | Uncharacterized protein yuab | protein | 128 | 2% helix, 55% strand | P71014 |
| B, D | Uncharacterized protein yuab | protein | 129 | 5% helix, 55% strand | P71014 |
| C, E, F | Uncharacterized protein yuab | protein | 130 | 2% helix, 56% strand | P71014 |
| I | Uncharacterized protein yuab | protein | 119 | 3% helix, 50% strand | P71014 |
| J | Uncharacterized protein yuab | protein | 118 | 3% helix, 50% strand | P71014 |
Ligands and binding sites
- CL · Chloride ion · ion · 10 copies · chains A, B, C, H, E, F, I
- GOL · Glycerol · additive · 6 copies · chains A, G, B, D, C, E, F, H, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.85 | 0.95 | 39 | empty |
| 2 | 687 | 0.81 | 0.85 | 81 | GOL |
| 3 | 334 | 0.75 | 0.86 | 41 | GOL |
| 4 | 463 | 0.74 | 0.83 | 59 | GOL |
| 5 | 228 | 0.71 | 0.87 | 32 | GOL |
Interfaces
26 interfaces between chains.
- F–H · 600 Ų buried · 6 hydrogen bonds · protein-protein
- C–E · 583 Ų buried · 5 hydrogen bonds · protein-protein
- A–G · 583 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 577 Ų buried · 7 hydrogen bonds · protein-protein
- C–H · 529 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 48 modified (methylation, engineered).
Compared structures
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 P71014
- Elsewhere: RCSB PDB 4BHU · PDBe 4BHU · UniProt P71014
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