Research workbench
Crystal structure of a bacterial bestrophin homolog from klebsiella pneumoniae D179A mutation - hr
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
- 6JLF
- Type
- protein
- Length
- 1,335 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 0.82
Structure
x-ray diffraction · 5 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bestrophin homolog | protein | 267 | 79% helix, 0% strand | W1ELP7 |
| B | Bestrophin homolog | protein | 266 | 80% helix, 0% strand | W1ELP7 |
| C | Bestrophin homolog | protein | 268 | 79% helix, 0% strand | W1ELP7 |
| D | Bestrophin homolog | protein | 268 | 82% helix, 0% strand | W1ELP7 |
| E | Bestrophin homolog | protein | 266 | 79% helix, 0% strand | W1ELP7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 11 copies · chains A, E, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.82 | 0.83 | 109 | empty |
| 2 | 53 | 0.71 | 0.98 | 15 | empty |
| 3 | 675 | 0.69 | 0.77 | 50 | ZN |
| 4 | 276 | 0.61 | 0.79 | 33 | empty |
| 5 | 253 | 0.59 | 0.79 | 39 | empty |
Interfaces
5 interfaces between chains.
- C–E · 2539 Ų buried · 18 hydrogen bonds · protein-protein
- A–E · 2488 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 2482 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 2463 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 2410 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 6JLF · Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae D179A… · 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 W1ELP7
- Elsewhere: RCSB PDB 6JLF · PDBe 6JLF · UniProt W1ELP7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.