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Zinc in PDB 6sey: Human Carbonic Anhydrase II in Complex with Aliphatically Substituted Benzenesulfonamide

Enzymatic activity of Human Carbonic Anhydrase II in Complex with Aliphatically Substituted Benzenesulfonamide

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

Protein crystallography data

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

Resolution Low / High (Å) 41.28 / 1.23
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.671, 41.842, 72.836, 90.00, 104.68, 90.00
R / Rfree (%) 11 / 12.5

Other elements in 6sey:

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

Mercury (Hg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II in Complex with Aliphatically Substituted Benzenesulfonamide (pdb code 6sey). 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 Aliphatically Substituted Benzenesulfonamide, PDB code: 6sey:

Zinc binding site 1 out of 1 in 6sey

Go back to Zinc Binding Sites List in 6sey
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with Aliphatically Substituted 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 Aliphatically Substituted Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:5.1
occ:1.00
 N A:L9B307 2.0 5.4 1.0
NE2 A:HIS94 2.0 5.2 1.0
ND1 A:HIS119 2.0 4.9 1.0
NE2 A:HIS96 2.1 5.1 1.0
CE1 A:HIS119 2.9 5.1 1.0
CD2 A:HIS94 3.0 5.0 1.0
O1 A:L9B307 3.0 6.3 1.0
CD2 A:HIS96 3.0 5.4 1.0
HE1 A:HIS119 3.0 6.1 1.0
S A:L9B307 3.1 6.1 1.0
CE1 A:HIS94 3.1 5.2 1.0
CE1 A:HIS96 3.1 6.2 1.0
CG A:HIS119 3.1 4.2 1.0
HD2 A:HIS94 3.2 6.0 1.0
HD2 A:HIS96 3.2 6.4 1.0
HB2 A:HIS119 3.2 5.4 1.0
HE1 A:HIS94 3.3 6.2 1.0
HE1 A:HIS96 3.3 7.4 1.0
CB A:HIS119 3.6 4.5 1.0
HG1 A:THR199 3.6 6.8 1.0
O A:HOH568 3.7 22.7 1.0
HB3 A:HIS119 3.7 5.4 1.0
OG1 A:THR199 3.9 5.6 1.0
OE1 A:GLU106 4.0 6.3 1.0
NE2 A:HIS119 4.1 5.1 1.0
O A:L9B307 4.1 6.7 1.0
ND1 A:HIS94 4.2 5.5 1.0
CG A:HIS94 4.2 5.5 1.0
ND1 A:HIS96 4.2 6.9 1.0
CG A:HIS96 4.2 5.1 1.0
C A:L9B307 4.2 7.3 1.0
CD2 A:HIS119 4.2 5.0 1.0
HH2 A:TRP209 4.2 7.3 1.0
HG23 A:THR200 4.8 11.8 1.0
C9 A:L9B307 4.8 8.6 1.0
HE2 A:HIS119 4.8 6.2 1.0
HG11 A:VAL143 4.9 7.6 1.0
HD1 A:HIS94 4.9 6.6 1.0
CD A:GLU106 5.0 6.5 1.0
HD1 A:HIS96 5.0 8.3 1.0
C1 A:L9B307 5.0 9.1 1.0

Reference:

S.Gloeckner, K.Ngo, A.Heine, G.Klebe. Human Carbonic Anhydrase II in Complex with Aliphatically Substituted Benzenesulfonamide To Be Published.
Page generated: Thu Aug 21 19:36:21 2025

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