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Zinc in PDB 1bcd: X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide

Enzymatic activity of X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide

All present enzymatic activity of X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide:
4.2.1.1;

Protein crystallography data

The structure of X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide, PDB code: 1bcd was solved by K.Hakansson, A.Liljas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide (pdb code 1bcd). 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 X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide, PDB code: 1bcd:

Zinc binding site 1 out of 1 in 1bcd

Go back to Zinc Binding Sites List in 1bcd
Zinc binding site 1 out of 1 in the X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Crystallographic Structure of A Complex Between Human Carbonic Anhydrase II and A New Topical Inhibitor, Trifluoromethane Sulphonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:6.3
occ:1.00
 ND1 A:HIS119 2.1 4.7 1.0
N A:FMS500 2.1 5.2 1.0
NE2 A:HIS94 2.2 5.1 1.0
NE2 A:HIS96 2.2 2.0 1.0
CE1 A:HIS119 2.9 3.6 1.0
CD2 A:HIS96 3.0 2.0 1.0
CD2 A:HIS94 3.1 4.7 1.0
CE1 A:HIS94 3.1 6.9 1.0
CG A:HIS119 3.1 3.4 1.0
S A:FMS500 3.2 7.8 1.0
CE1 A:HIS96 3.3 2.6 1.0
F1 A:FMS500 3.4 6.0 1.0
O2 A:FMS500 3.5 6.2 1.0
CB A:HIS119 3.6 2.0 1.0
C A:FMS500 3.8 7.0 1.0
NE2 A:HIS119 4.0 4.0 1.0
OG1 A:THR199 4.0 2.7 1.0
OE1 A:GLU106 4.1 6.1 1.0
CD2 A:HIS119 4.2 3.4 1.0
CG A:HIS94 4.2 5.0 1.0
CG A:HIS96 4.2 2.0 1.0
ND1 A:HIS94 4.2 4.3 1.0
F3 A:FMS500 4.3 5.8 1.0
ND1 A:HIS96 4.3 2.7 1.0
O1 A:FMS500 4.4 5.8 1.0
F2 A:FMS500 5.0 9.2 1.0
CD A:GLU106 5.0 5.8 1.0

Reference:

K.Hakansson, A.Liljas. The Structure of A Complex Between Carbonic Anhydrase II and A New Inhibitor, Trifluoromethane Sulphonamide. Febs Lett. V. 350 319 1994.
ISSN: ISSN 0014-5793
PubMed: 8070585
DOI: 10.1016/0014-5793(94)00798-5
Page generated: Fri Sep 25 21:03:22 2020
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