MolNFT v2 · #145091 · protein
Vps4p-Vta1p complex with peptide binding to the central pore of Vps4p
6BMF: “Vps4p-Vta1p complex with peptide binding to the central pore of Vps4p”. Electron microscopy at 3.2, 3 ligands (ADP, BEF, MG). MolNFT v2 #145091 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6BMF
- Type
- protein
- Length
- 1,407 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2
- Source
- Saccharomyces cerevisiae; SYNTHETIC CONSTRUCT
- UniProt
- P52917
- Ligands
- ADP, BEF, MG
Structure
electron microscopy · resolution 3.2 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 277 | — | P52917 |
| B, C, D | — | protein | 285 | — | P52917 |
| E | — | protein | 267 | — | P52917 |
| G | — | protein | 8 | — | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, E
- BEF · Beryllium trifluoride ion · ligand · 3 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BMF · VPS4P-VTA1P complex with peptide binding to the central pore of VPS4P · 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 P52917
- Elsewhere: RCSB PDB 6BMF · PDBe 6BMF · UniProt P52917
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