MolNFT v2 · #152057 · protein
Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1
6HD3: “Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1”. X-ray diffraction at 2.8, 2 ligands (ADP, PO4). MolNFT v2 #152057 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HD3
- Type
- protein
- Length
- 885 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- Arabidopsis thaliana
- UniProt
- P54609
- Ligands
- ADP, PO4
Structure
x-ray diffraction · resolution 2.8 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 450 | — | P54609 |
| C | — | protein | 435 | — | P54609 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, C
- PO4 · Phosphate ion · ion · 3 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HD3 · Common mode of remodeling aaa atpases P97/CDC48 by their disassembly cofactors ASPL/PUX1 · the same entry in another collection · chain A against A, TM-score 1.00
- P54609 · AlphaFold monomer V2.0 prediction for cell division control protein 48 homolog a (P54609) · a predicted model of the same protein · chain C against A, TM-score 0.71
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 P54609
- Elsewhere: RCSB PDB 6HD3 · PDBe 6HD3 · UniProt P54609
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