Research workbench
Cryo-EM structure of DNF1 from saccharomyces cerevisiae in yeast lipids with beryllium fluoride (resting state)
Analyse Cryo-EM structure of DNF1 from saccharomyces cerevisiae in yeast lipids with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F7F
- Type
- protein
- Length
- 1,497 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P32660, P42838
- Ligands
- NAG, BMA, MG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1135 | — | P32660 |
| B | — | protein | 362 | — | P42838 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains B, A
- BMA · beta-D-mannopyranose · sugar
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7F7F · Cryo-EM structure of Dnf1 from Saccharomyces cerevisiae in yeast lipids with beryllium… · the same entry in another collection · chain A against A, TM-score 1.00
- P42838 · AlphaFold monomer V2.0 prediction for alkylphosphocholine resistance protein LEM3 (P42838) · a predicted model of the same protein · chain B against A, TM-score 0.96
- P32660 · AlphaFold monomer V2.0 prediction for phospholipid-transporting ATPase DNF1 (P32660) · a predicted model of the same protein · chain A against A, TM-score 0.72
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 P32660
- Every structure of UniProt P42838
- Elsewhere: RCSB PDB 7F7F · PDBe 7F7F · UniProt P32660 · UniProt P42838
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