MolNFT v2 · #138143 · protein
Open conformation of KcsA deep-inactivated
5VKE: “Open conformation of KcsA deep-inactivated”. X-ray diffraction at 2.37, 3 ligands (F09, 1EM, K). MolNFT v2 #138143 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5VKE
- Type
- protein
- Length
- 527 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.37
- Source
- Mus musculus; Streptomyces lividans
- UniProt
- P0A334
- Ligands
- F09, 1EM, K
Structure
x-ray diffraction · resolution 2.37 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 219 | — | — |
| B | — | protein | 212 | — | — |
| C | — | protein | 96 | — | P0A334 |
Ligands and binding sites
- F09 · Nonan-1-ol · ligand · chains A, C
- 1EM · (1S)-2-hydroxy-1-[(nonanoyloxy)methyl]ethyl myristate · ligand · chains C
- K · Potassium ion · metal · 3 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VKE · Open conformation of kcsa deep-inactivated · 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 P0A334
- Elsewhere: RCSB PDB 5VKE · PDBe 5VKE · UniProt P0A334
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