MolNFT v1 · #190388 · protein
Cryo-EM structure of NA+,K+-ATPase in the E2P state formed by inorganic phosphate
7WYW: “Cryo-EM structure of NA+,K+-ATPase in the E2P state formed by inorganic phosphate”. Electron microscopy, 7 ligands (PCW, CLR, NAG). MolNFT v1 #190388 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7WYW
- Type
- protein
- Length
- 2,654 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4H132, C4IX13, Q70Q12
- Ligands
- PCW, CLR, NAG, MAN, BMA, FUC, MG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 993 | — | Q4H132 |
| B, D | — | protein | 294 | — | C4IX13 |
| G, E | — | protein | 40 | — | Q70Q12 |
Ligands and binding sites
- PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 24 copies · chains A, G, B, C, D, E
- CLR · Cholesterol · ligand · 8 copies · chains A, G, B, C, E, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 18 copies · chains B, D
- MAN · alpha-D-mannopyranose · sugar · 10 copies · chains B, D
- BMA · beta-D-mannopyranose · sugar · 6 copies
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains B, D
- MG · Magnesium ion · metal · 6 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WYW · Cryo-EM structure of Na+,K+-ATPase in the E2P state formed by inorganic phosphate · 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 Q4H132
- Every structure of UniProt C4IX13
- Every structure of UniProt Q70Q12
- Elsewhere: RCSB PDB 7WYW · PDBe 7WYW · UniProt Q4H132 · UniProt C4IX13 · UniProt Q70Q12
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