9GUM | pdb_00009gum

Human carbonic anhydrase II complexed with N-phenethyl-2-(1H-tetrazol-5-yl)acetamide


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 
    0.248 (Depositor), 0.244 (DCC) 
  • R-Value Work: 
    0.153 (Depositor), 0.164 (DCC) 

Starting Model: experimental
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Literature

Tetrazole Is a Novel Zinc Binder Chemotype for Carbonic Anhydrase Inhibition.

Giovannuzzi, S.Angeli, A.Begines, P.Ferraroni, M.Nocentini, A.Supuran, C.T.

(2025) ACS Med Chem Lett 16: 163-166

  • DOI: https://doi.org/10.1021/acsmedchemlett.4c00562
  • Primary Citation of Related Structures:  
    9GU7, 9GUM, 9GUO

  • PubMed Abstract: 

    The tetrazole group is here proposed as a zinc-binding warhead for the inhibition of the metalloenzyme carbonic anhydrases. A set of synthesized derivatives incorporating the tetrazole moiety were evaluated as inhibitors against a panel of human isoforms, exhibiting K I values spanning between the submicromolar and low-to-medium micromolar ranges (0.62-19.6 μM). X-ray crystallographic studies were conducted to gain insights into their modes of binding to the target enzyme. These findings mark a significant advancement in the search for inhibitory chemotypes other than classical sulfonamides.


  • Organizational Affiliation

    NEUROFARBA Department, Section of Pharmaceutical Science, University of Florence, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbonic anhydrase 2A [auth AAA]260Homo sapiensMutation(s): 0 
Gene Names: CA2
EC: 4.2.1.1 (PDB Primary Data), 4.2.1.69 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P00918 (Homo sapiens)
Explore P00918 
Go to UniProtKB:  P00918
PHAROS:  P00918
GTEx:  ENSG00000104267 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00918
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free:  0.248 (Depositor), 0.244 (DCC) 
  • R-Value Work:  0.153 (Depositor), 0.164 (DCC) 
Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.568α = 90
b = 41.876β = 104.732
c = 72.564γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
REFMACphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2025-07-02
    Type: Initial release