MolNFT v1 · #160734 · protein
Cryo-EM structure of S. cerevisiae DRS2P-CDC50P in the PI4P-activated form
6PSX: “Cryo-EM structure of S. cerevisiae DRS2P-CDC50P in the PI4P-activated form”. Electron microscopy, 1 ligand (NAG). MolNFT v1 #160734 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PSX
- Type
- protein
- Length
- 1,372 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39524, P25656
- Ligands
- NAG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1033 | — | P39524 |
| E | — | protein | 339 | — | P25656 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PSX · Cryo-EM structure of S. cerevisiae Drs2p-Cdc50p in the PI4P-activated form · the same entry in another collection · chain A against A, TM-score 1.00
- P25656 · AlphaFold monomer V2.0 prediction for cell division control protein 50 (P25656) · a predicted model of the same protein · chain E against A, TM-score 0.97
- P39524 · AlphaFold monomer V2.0 prediction for probable phospholipid- transporting ATPase DRS2… · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P39524
- Every structure of UniProt P25656
- Elsewhere: RCSB PDB 6PSX · PDBe 6PSX · UniProt P39524 · UniProt P25656
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