Research workbench
Crystal structure of CRISPR-associated protein
Analyse Crystal structure of CRISPR-associated protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VZI
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CRISPR-associated protein CAS5, dvulg subtype
- UniProt
- B2SNP4
- Pockets
- 5 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CRISPR-associated protein CAS5, dvulg subtype | protein | 214 | 21% helix, 35% strand | B2SNP4 |
| B | CRISPR-associated protein CAS5, dvulg subtype | protein | 213 | 21% helix, 35% strand | B2SNP4 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.61 | 0.85 | 28 | empty |
| 2 | 124 | 0.53 | 0.82 | 26 | empty |
| 3 | 91 | 0.47 | 0.81 | 29 | empty |
| 4 | 147 | 0.40 | 0.74 | 30 | empty |
| 5 | 100 | 0.36 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 658 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3VZI · Crystal Structure of CRISPR-associated Protein · 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 B2SNP4
- Elsewhere: RCSB PDB 3VZI · PDBe 3VZI · UniProt B2SNP4
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