MolNFT v1 · #87521 · protein
The carbonic anhydrase from thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme
4C3T · Carbonate dehydratase: “The carbonic anhydrase from thermovibrio ammonificans reveals an interesting intermolecular disulfide…”. X-ray diffraction, 2 ligands (ZN, CL), 2 pockets (best druggability 0.48). MolNFT v1 #87521 on…
- 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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