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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCarbonate dehydratase (EC 4.2.1.1)protein22517% helix, 33% strandE8T502

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A, B

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11080.480.8022empty
21110.470.7922empty

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

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