Research workbench
Dpbb domain of vcp-like ATPase from methanopyrus kandleri
Analyse Dpbb domain of vcp-like ATPase from methanopyrus kandleri in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DG7
- Type
- protein
- Length
- 86 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATPase of the aaa+ class
- UniProt
- Q8TY20
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATPase of the aaa+ class | protein | 86 | 23% helix, 40% strand | Q8TY20 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7DG7 · DPBB domain of VCP-like ATPase from Methanopyrus kandleri · 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 Q8TY20
- Elsewhere: RCSB PDB 7DG7 · PDBe 7DG7 · UniProt Q8TY20
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