Atomistry » Zinc » PDB 6rg4-6rpc » 6rnp
Atomistry »
  Zinc »
    PDB 6rg4-6rpc »
      6rnp »

Zinc in PDB 6rnp: Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide

Enzymatic activity of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide, PDB code: 6rnp was solved by S.Gloeckner, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.97 / 1.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.325, 41.454, 72.291, 90.00, 104.53, 90.00
R / Rfree (%) 11.9 / 13.6

Other elements in 6rnp:

The structure of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Mercury (Hg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide (pdb code 6rnp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide, PDB code: 6rnp:

Zinc binding site 1 out of 1 in 6rnp

Go back to Zinc Binding Sites List in 6rnp
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II in Complex with Fluorinated Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:6.8
occ:1.00
 N A:KBB303 2.0 6.4 1.0
NE2 A:HIS94 2.0 6.8 1.0
ND1 A:HIS119 2.0 6.7 1.0
NE2 A:HIS96 2.0 7.2 1.0
CE1 A:HIS119 2.9 6.6 1.0
CD2 A:HIS96 3.0 7.8 1.0
CD2 A:HIS94 3.0 6.9 1.0
CE1 A:HIS94 3.0 7.0 1.0
O A:KBB303 3.0 7.8 1.0
CE1 A:HIS96 3.0 7.4 1.0
HE1 A:HIS119 3.1 7.9 1.0
S A:KBB303 3.1 7.2 1.0
CG A:HIS119 3.1 6.4 1.0
HD2 A:HIS96 3.1 9.4 1.0
HD2 A:HIS94 3.2 8.3 1.0
HB2 A:HIS119 3.2 8.5 1.0
HE1 A:HIS94 3.2 8.5 1.0
HE1 A:HIS96 3.3 8.9 1.0
CB A:HIS119 3.6 7.1 1.0
HG1 A:THR199 3.6 8.9 1.0
O A:HOH594 3.6 16.2 1.0
HB3 A:HIS119 3.7 8.5 1.0
OG1 A:THR199 3.9 7.4 1.0
OE1 A:GLU106 4.0 7.4 1.0
NE2 A:HIS119 4.1 7.1 1.0
O1 A:KBB303 4.1 7.8 1.0
ND1 A:HIS94 4.1 7.5 1.0
ND1 A:HIS96 4.1 8.5 1.0
CG A:HIS96 4.1 7.7 1.0
CG A:HIS94 4.1 7.2 1.0
HH2 A:TRP209 4.2 10.1 1.0
CD2 A:HIS119 4.2 6.8 1.0
C A:KBB303 4.2 8.2 1.0
O A:HOH592 4.8 28.9 1.0
HE2 A:HIS119 4.8 8.5 1.0
F1 A:KBB303 4.9 8.8 1.0
HG11 A:VAL143 4.9 9.4 1.0
HG23 A:THR200 4.9 12.9 1.0
HD1 A:HIS94 4.9 9.0 1.0
CD A:GLU106 4.9 7.4 1.0
HD1 A:HIS96 4.9 10.2 1.0
C5 A:KBB303 5.0 7.9 1.0
C1 A:KBB303 5.0 8.7 1.0

Reference:

S.Glockner, K.Ngo, B.Wagner, A.Heine, G.Klebe. The Influence of Varying Fluorination Patterns on the Thermodynamics and Kinetics of Benzenesulfonamide Binding to Human Carbonic Anhydrase II. Biomolecules V. 10 2020.
ISSN: ESSN 2218-273X
PubMed: 32230853
DOI: 10.3390/BIOM10040509
Page generated: Tue Oct 29 06:39:58 2024

Last articles

Na in 1UBS
Na in 1U8R
Na in 1U7H
Na in 1U4J
Na in 1TW8
Na in 1TX3
Na in 1U02
Na in 1TY8
Na in 1TXZ
Na in 1TQY
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy