Research workbench
Structure of the S. cerevisiae P4B ATPase lipid flippase in the E2P state
Analyse Structure of the S. cerevisiae P4B ATPase lipid flippase in the E2P state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RD6
- Type
- protein
- Length
- 929 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P40527
- Ligands
- BEF, MG
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 929 | — | P40527 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7RD6 · Structure of the S. cerevisiae P4B ATPase lipid flippase in the E2P state · the same entry in another collection · chain A against A, TM-score 1.00
- P40527 · AlphaFold monomer V2.0 prediction for probable phospholipid- transporting ATPase NEO1… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P40527
- Elsewhere: RCSB PDB 7RD6 · PDBe 7RD6 · UniProt P40527
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