Zinc in PDB 5je7: Human Carbonic Anhydrase II (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide

Enzymatic activity of Human Carbonic Anhydrase II (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide

All present enzymatic activity of Human Carbonic Anhydrase II (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide, PDB code: 5je7 was solved by J.M.Fox, K.Kang, M.Sastry, W.Sherman, B.Sankaran, P.H.Zwart, G.M.Whitesides, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.43 / 1.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.480, 41.720, 72.570, 90.00, 104.71, 90.00
R / Rfree (%) 12.2 / 14.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide (pdb code 5je7). 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 (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide, PDB code: 5je7:

Zinc binding site 1 out of 1 in 5je7

Go back to Zinc Binding Sites List in 5je7
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide


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 (F131Y) Complexed with Benzo[D]Thiazole-2- Sulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:4.5
occ:1.00
HNA B:EVF302 1.3 6.0 1.0
N B:EVF302 2.0 5.0 1.0
NE2 B:HIS94 2.0 3.9 1.0
ND1 B:HIS119 2.0 4.4 1.0
NE2 B:HIS96 2.0 4.5 1.0
HN B:EVF302 2.4 6.0 1.0
CE1 B:HIS119 2.9 4.7 1.0
CD2 B:HIS94 3.0 4.1 1.0
CD2 B:HIS96 3.0 4.5 1.0
CE1 B:HIS94 3.0 4.2 1.0
O2 B:EVF302 3.0 5.5 1.0
CE1 B:HIS96 3.1 5.5 1.0
S B:EVF302 3.1 5.7 1.0
HE1 B:HIS119 3.1 5.7 1.0
CG B:HIS119 3.1 4.3 1.0
HD2 B:HIS94 3.2 5.0 1.0
HD2 B:HIS96 3.2 5.4 1.0
HB2 B:HIS119 3.2 5.0 1.0
HE1 B:HIS94 3.2 5.0 1.0
HE1 B:HIS96 3.3 6.7 1.0
CB B:HIS119 3.6 4.2 1.0
HG1 B:THR198 3.6 5.6 1.0
HB3 B:HIS119 3.7 5.0 1.0
O B:HOH616 3.8 8.5 1.0
OG1 B:THR198 3.9 4.7 1.0
OE1 B:GLU106 4.0 5.2 1.0
O1 B:EVF302 4.1 5.9 1.0
NE2 B:HIS119 4.1 4.7 1.0
ND1 B:HIS94 4.1 4.0 1.0
CG B:HIS94 4.1 3.7 1.0
ND1 B:HIS96 4.1 5.5 1.0
CG B:HIS96 4.2 4.6 1.0
C2 B:EVF302 4.2 7.3 1.0
CD2 B:HIS119 4.2 4.6 1.0
HH2 B:TRP208 4.2 7.3 1.0
O B:HOH730 4.3 20.8 1.0
HE2 B:HIS119 4.9 5.7 1.0
CD B:GLU106 4.9 5.3 1.0
HD1 B:HIS94 4.9 4.9 1.0
HD1 B:HIS96 4.9 6.7 1.0
N3 B:EVF302 5.0 6.7 1.0
HG11 B:VAL142 5.0 6.8 1.0

Reference:

J.M.Fox, K.Kang, M.Sastry, W.Sherman, B.Sankaran, P.H.Zwart, G.M.Whitesides. Water-Restructuring Mutations Can Reverse the Thermodynamic Signature of Ligand Binding to Human Carbonic Anhydrase. Angew. Chem. Int. Ed. Engl. V. 56 3833 2017.
ISSN: ESSN 1521-3773
PubMed: 28252841
DOI: 10.1002/ANIE.201609409
Page generated: Wed Dec 16 06:24:53 2020

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