Research workbench
A core mutation affecting the folding properties of a soluble domain of the ATPase protein copa from bacillus subtilis
Analyse A core mutation affecting the folding properties of a soluble domain of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OPZ
- Type
- protein
- Length
- 76 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potential copper-transporting ATPase
- EC
- 3.6.3.4
- UniProt
- O32220
Structure
solution nmr · 1 distinct chain · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potential copper-transporting ATPase (EC 3.6.3.4) | protein | 76 | 32% helix, 32% strand | O32220 |
Compared structures
- 1OPZ · A core mutation affecting the folding properties of a soluble domain of the ATPase… · the same entry in another collection · chain A against A, TM-score 1.00
- O32220 · AlphaFold monomer V2.0 prediction for copper-exporting P-type ATPase (O32220) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 O32220
- Elsewhere: RCSB PDB 1OPZ · PDBe 1OPZ · UniProt O32220
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