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Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole Degradation (CarC enzyme)
Analyse Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J1I
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.86
- Source
- Janthinobacterium
- Molecule
- meta cleavage compound hydrolase
- EC
- 3.7.1.8
- UniProt
- Q84II3
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · resolution 1.86 · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | meta cleavage compound hydrolase (EC 3.7.1.8) | protein | 258 | 43% helix, 20% strand | Q84II3 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 265 | 0.56 | 0.77 | 32 | empty |
| 2 | 57 | 0.35 | 0.78 | 17 | empty |
Compared structures
- 1J1I · Crystal structure of a his-tagged serine hydrolase involved in the carbazole degradation… · 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 Q84II3
- Elsewhere: RCSB PDB 1J1I · PDBe 1J1I · UniProt Q84II3
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