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Zinc in PDB 6sbh: Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.

Enzymatic activity of Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide., PDB code: 6sbh 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) 34.93 / 0.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.294, 41.530, 72.165, 90.00, 104.52, 90.00
R / Rfree (%) 12 / 13.4

Other elements in 6sbh:

The structure of Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide. 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 4- Pentylbenzenesulfonamide. (pdb code 6sbh). 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 4- Pentylbenzenesulfonamide., PDB code: 6sbh:

Zinc binding site 1 out of 1 in 6sbh

Go back to Zinc Binding Sites List in 6sbh
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with 4- Pentylbenzenesulfonamide.


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 4- Pentylbenzenesulfonamide. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:5.3
occ:1.00
 N A:L4K304 2.0 6.0 1.0
NE2 A:HIS94 2.0 5.8 1.0
NE2 A:HIS96 2.0 5.8 1.0
ND1 A:HIS119 2.0 5.2 1.0
CE1 A:HIS119 2.9 5.5 1.0
CD2 A:HIS94 3.0 5.8 1.0
CD2 A:HIS96 3.0 5.7 1.0
O1 A:L4K304 3.0 6.6 1.0
CE1 A:HIS94 3.0 6.0 1.0
S A:L4K304 3.0 5.8 1.0
CE1 A:HIS96 3.0 6.4 1.0
HE1 A:HIS119 3.1 6.6 1.0
CG A:HIS119 3.1 5.4 1.0
HD2 A:HIS96 3.1 6.9 1.0
HD2 A:HIS94 3.2 7.0 1.0
HB2 A:HIS119 3.2 6.5 1.0
HE1 A:HIS94 3.2 7.1 1.0
HE1 A:HIS96 3.3 7.6 1.0
HG1 A:THR199 3.5 6.9 1.0
CB A:HIS119 3.6 5.4 1.0
O A:HOH556 3.7 17.6 1.0
HB3 A:HIS119 3.7 6.5 1.0
OG1 A:THR199 3.9 5.7 1.0
OE1 A:GLU106 4.0 6.2 1.0
O A:L4K304 4.1 6.6 1.0
NE2 A:HIS119 4.1 5.3 1.0
ND1 A:HIS94 4.1 6.3 1.0
CG A:HIS94 4.2 6.0 1.0
ND1 A:HIS96 4.2 7.0 1.0
CG A:HIS96 4.2 6.0 1.0
HH2 A:TRP209 4.2 7.5 1.0
C8 A:L4K304 4.2 6.6 1.0
CD2 A:HIS119 4.2 5.5 1.0
HG23 A:THR200 4.8 11.9 1.0
C7 A:L4K304 4.8 8.1 1.0
HE2 A:HIS119 4.9 6.3 1.0
HG11 A:VAL143 4.9 7.9 1.0
CD A:GLU106 4.9 5.9 1.0
HD1 A:HIS94 4.9 7.6 1.0
HD1 A:HIS96 4.9 8.4 1.0
C9 A:L4K304 5.0 7.2 1.0

Reference:

S.Glockner, K.Ngo, C.P.Sager, T.Hufner-Wulsdorf, A.Heine, G.Klebe. Conformational Changes in Alkyl Chains Determine the Thermodynamic and Kinetic Binding Profiles of Carbonic Anhydrase Inhibitors. Acs Chem.Biol. V. 15 675 2020.
ISSN: ESSN 1554-8937
PubMed: 32027480
DOI: 10.1021/ACSCHEMBIO.9B00895
Page generated: Thu Aug 21 19:30:35 2025

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