4Q6D

Crystal structure of human carbonic anhydrase isozyme II with 4-[(Z)-azepan-1-yldiazenyl]benzenesulfonamide


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.12 Å
  • R-Value Free: 0.154 
  • R-Value Work: 0.128 
  • R-Value Observed: 0.131 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

4-Amino-substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases.

Rutkauskas, K.Zubriene, A.Tumosiene, I.Kantminiene, K.Kazemekaite, M.Smirnov, A.Kazokaite, J.Morkunaite, V.Capkauskaite, E.Manakova, E.Grazulis, S.Beresnevicius, Z.J.Matulis, D.

(2014) Molecules 19: 17356-17380

  • DOI: https://doi.org/10.3390/molecules191117356
  • Primary Citation of Related Structures:  
    4Q6D, 4Q6E

  • PubMed Abstract: 

    A series of N-aryl-β-alanine derivatives and diazobenzenesulfonamides containing aliphatic rings were designed, synthesized, and their binding to carbonic anhydrases (CA) I, II, VI, VII, XII, and XIII was studied by the fluorescent thermal shift assay and isothermal titration calorimetry. The results showed that 4-substituted diazobenzenesulfonamides were more potent CA binders than N-aryl-β-alanine derivatives. Most of the N-aryl-β-alanine derivatives showed better affinity for CA II while diazobenzenesulfonamides possessed nanomolar affinities towards CA I isozyme. X-ray crystallographic structures showed the modes of binding of both compound groups.


  • Organizational Affiliation

    Department of Organic Chemistry, Kaunas University of Technology, Kaunas LT-50254, Lithuania. kestutis.rutkauskas@ktu.lt.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbonic anhydrase 2260Homo sapiensMutation(s): 0 
Gene Names: CA2
EC: 4.2.1.1
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
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
WW3 Binding MOAD:  4Q6D Kd: 43.5 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.12 Å
  • R-Value Free: 0.154 
  • R-Value Work: 0.128 
  • R-Value Observed: 0.131 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.125α = 90
b = 41.195β = 104.19
c = 71.813γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
SCALAdata scaling
PDB_EXTRACTdata extraction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-11-26
    Type: Initial release
  • Version 1.1: 2018-03-07
    Changes: Advisory, Data collection
  • Version 1.2: 2023-09-20
    Changes: Advisory, Data collection, Database references, Derived calculations, Refinement description