Research workbench
The carbonic anhydrase from thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme
Analyse The carbonic anhydrase from thermovibrio ammonificans reveals an interesting… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C3T
- Type
- protein
- Length
- 450 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonate dehydratase
- EC
- 4.2.1.1
- UniProt
- E8T502
- Ligands
- ZN, CL
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbonate dehydratase (EC 4.2.1.1) | protein | 225 | 17% helix, 33% strand | E8T502 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.48 | 0.80 | 22 | empty |
| 2 | 111 | 0.47 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 65 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4C3T · The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting… · 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 E8T502
- Elsewhere: RCSB PDB 4C3T · PDBe 4C3T · UniProt E8T502
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