Research workbench
Hnh nuclease domain from G. stearothermophilus CAS9
Analyse Hnh nuclease domain from G. stearothermophilus CAS9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MPZ
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated endonuclease CAS9
- EC
- 3.1.-.-
- UniProt
- A0A250DVH8
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated endonuclease CAS9 (EC 3.1.-.-) | protein | 138 | 54% helix, 9% strand | A0A250DVH8 |
Compared structures
- 7MPZ · HNH Nuclease Domain from G. stearothermophilus Cas9 · 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 A0A250DVH8
- Elsewhere: RCSB PDB 7MPZ · PDBe 7MPZ · UniProt A0A250DVH8
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