Research workbench
Crystal structure of a bacterial bestrophin homolog from klebsiella pneumoniae with a mutation D269A
Analyse Crystal structure of a bacterial bestrophin homolog from klebsiella pneumoniae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IVW
- Type
- protein
- Length
- 1,337 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bestrophin homolog
- UniProt
- W1ELP7
- Ligands
- ZN
- Pockets
- 17 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Bestrophin homolog | protein | 268 | 76% helix, 0% strand | W1ELP7 |
| B | Bestrophin homolog | protein | 266 | 78% helix, 0% strand | W1ELP7 |
| C | Bestrophin homolog | protein | 265 | 78% helix, 0% strand | W1ELP7 |
| E | Bestrophin homolog | protein | 270 | 74% helix, 0% strand | W1ELP7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 9 copies · chains A, E, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1094 | 0.83 | 0.83 | 127 | empty |
| 2 | 82 | 0.72 | 0.96 | 22 | empty |
| 3 | 624 | 0.70 | 0.79 | 51 | empty |
| 4 | 72 | 0.69 | 0.94 | 17 | empty |
| 5 | 311 | 0.62 | 0.79 | 31 | empty |
Interfaces
8 interfaces between chains.
- A–E · 2658 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 2645 Ų buried · 22 hydrogen bonds · protein-protein
- B–D · 2603 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 2533 Ų buried · 20 hydrogen bonds · protein-protein
- C–E · 2416 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6IVW · Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a… · the same entry in another collection · chain E against E, 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 W1ELP7
- Elsewhere: RCSB PDB 6IVW · PDBe 6IVW · UniProt W1ELP7
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