1G52

CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.165 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Contribution of Fluorine to Protein-Ligand Affinity in the Binding of Fluoroaromatic Inhibitors to Carbonic Anhydrase II

Kim, C.-Y.Chang, J.S.Doyon, J.B.Baird Jr., T.T.Fierke, C.A.Jain, A.Christianson, D.W.

(2000) J Am Chem Soc 122: 12125-12134


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CARBONIC ANHYDRASE II259Homo sapiensMutation(s): 0 
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
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
F2B
Query on F2B

Download Ideal Coordinates CCD File 
D [auth A]N-(2,3-DIFLUORO-BENZYL)-4-SULFAMOYL-BENZAMIDE
C14 H12 F2 N2 O3 S
QASSMVGOSBNFQY-UHFFFAOYSA-N
HG
Query on HG

Download Ideal Coordinates CCD File 
C [auth A]MERCURY (II) ION
Hg
BQPIGGFYSBELGY-UHFFFAOYSA-N
ZN
Query on ZN

Download Ideal Coordinates CCD File 
B [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
F2B BindingDB:  1G52 Kd: 1.6 (nM) from 1 assay(s)
PDBBind:  1G52 Kd: 0.29 (nM) from 1 assay(s)
Binding MOAD:  1G52 Kd: 0.29 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.165 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.75α = 90
b = 41.87β = 104.88
c = 72.22γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-11-08
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection
  • Version 1.4: 2018-10-31
    Changes: Data collection, Database references
  • Version 1.5: 2024-02-07
    Changes: Data collection, Database references, Derived calculations