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Structure, refinement and function of carbonic anhydrase isozymes. refinement of human carbonic anhydrase I

Analyse Structure, refinement and function of carbonic anhydrase isozymes. refinement… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2CAB
Type
protein
Length
256 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Homo sapiens
Molecule
Carbonic anhydrase form B
EC
4.2.1.1
UniProt
P00915
Ligands
ZN
Pockets
2 · best druggability 0.52

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 16% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarbonic anhydrase form B (EC 4.2.1.1)protein25616% helix, 32% strandP00915

Ligands and binding sites

  • ZN · Zinc ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.520.8021empty
2720.370.7714empty

Compared structures

  • 2CAB · Structure, refinement and function of carbonic anhydrase isozymes. refinement of human… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00915 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 1 (P00915) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

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