Research workbench
Structure of the mit domain from a S. solfataricus VPS4- like ATPase
Analyse Structure of the mit domain from a S. solfataricus VPS4- like ATPase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V6Y
- Type
- protein
- Length
- 147 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aaa family ATPase, P60 katanin
- EC
- 3.6.4.6
- UniProt
- Q97ZJ7
- Ligands
- SRT
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aaa family ATPase, P60 katanin (EC 3.6.4.6) | protein | 75 | 80% helix, 0% strand | Q97ZJ7 |
| B | Aaa family ATPase, P60 katanin (EC 3.6.4.6) | protein | 72 | 81% helix, 0% strand | Q97ZJ7 |
Ligands and binding sites
- SRT · S,R meso-tartaric acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2V6Y · Structure of the MIT domain from a S. solfataricus Vps4-like ATPase · 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 Q97ZJ7
- Elsewhere: RCSB PDB 2V6Y · PDBe 2V6Y · UniProt Q97ZJ7
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