Research workbench
Structure of the Vibrio cholerae di-nucleotide cyclase (DncV) mutant D131A-D133A
Analyse Structure of the Vibrio cholerae di-nucleotide cyclase (DncV) mutant D131A-D133A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U0L
- Type
- protein
- Length
- 769 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Vibrio cholerae El Tor N16961
- Molecule
- Cyclic AMP-GMP synthase
- EC
- 2.7.7.86
- UniProt
- Q9KVG7
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · resolution 2.1 · 2 distinct chains · 56% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic AMP-GMP synthase (EC 2.7.7.86) | protein | 386 | 56% helix, 13% strand | Q9KVG7 |
| B | Cyclic AMP-GMP synthase (EC 2.7.7.86) | protein | 383 | 55% helix, 13% strand | Q9KVG7 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 607 | 0.67 | 0.76 | 52 | empty |
| 2 | 620 | 0.66 | 0.76 | 51 | empty |
| 3 | 447 | 0.64 | 0.77 | 38 | empty |
| 4 | 238 | 0.52 | 0.76 | 24 | empty |
| 5 | 64 | 0.31 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 476 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4U0L · Structure of the vibrio cholerae di-nucleotide cyclase (dncv) mutant D131A-D133A · the same entry in another collection · chain A against A, TM-score 1.00
- Q9KVG7 · AlphaFold monomer V2.0 prediction for cyclic gmp-AMP synthase (Q9KVG7) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9KVG7
- Elsewhere: RCSB PDB 4U0L · PDBe 4U0L · UniProt Q9KVG7
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