MolNFT v2 · #153830 · protein
Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a mutation Y211A
6IV2: “Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a mutation Y211A”. X-ray diffraction at 2.62, 1 ligand (ZN). MolNFT v2 #153830 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6IV2
- Type
- protein
- Length
- 1,329 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.62
- Source
- Klebsiella pneumoniae IS53
- UniProt
- W1ELP7
- Ligands
- ZN
Structure
x-ray diffraction · resolution 2.62 · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 267 | — | W1ELP7 |
| B | — | protein | 267 | — | W1ELP7 |
| C | — | protein | 262 | — | W1ELP7 |
| D | — | protein | 268 | — | W1ELP7 |
| E | — | protein | 265 | — | W1ELP7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 12 copies · chains A, E, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IV2 · Crystal structure of a bacterial bestrophin homolog from klebsiella pneumoniae with a… · 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 6IV2 · PDBe 6IV2 · UniProt W1ELP7
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