Research workbench
Structure of the fungal plasma membrane proton pump PMA1 in its auto- inhibited state - hexameric assembly
Analyse Structure of the fungal plasma membrane proton pump PMA1 in its auto- inhibited… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NY1
- Type
- protein
- Length
- 4,974 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0B0DXJ0
- Ligands
- ADP, MG, K
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 829 | — | A0A0B0DXJ0 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · 6 copies · chains A, B, C, D, E, F
- K · Potassium ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NY1 · Structure of the fungal plasma membrane proton pump Pma1 in its auto-inhibited state… · 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 A0A0B0DXJ0
- Elsewhere: RCSB PDB 7NY1 · PDBe 7NY1 · UniProt A0A0B0DXJ0
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