Research workbench
Halogenase domain from cura module (crystal form IV)
Analyse Halogenase domain from cura module (crystal form IV) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NNM
- Type
- protein
- Length
- 636 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cura
- UniProt
- Q6DNF2
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cura | protein | 318 | 42% helix, 19% strand | Q6DNF2 |
Ligands and binding sites
- FMT · Formic acid · additive · 13 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.69 | 0.90 | 30 | FMT |
| 2 | 117 | 0.66 | 0.89 | 30 | FMT |
| 3 | 506 | 0.62 | 0.75 | 49 | FMT |
| 4 | 128 | 0.52 | 0.81 | 23 | FMT |
| 5 | 123 | 0.48 | 0.79 | 24 | FMT |
Interfaces
1 interface between chains.
- A–B · 979 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3NNM · Halogenase domain from CurA module (crystal form IV) · 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 Q6DNF2
- Elsewhere: RCSB PDB 3NNM · PDBe 3NNM · UniProt Q6DNF2
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