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Zinc in PDB 2nxs: Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II

Enzymatic activity of Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II

All present enzymatic activity of Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II, PDB code: 2nxs was solved by S.Z.Fisher, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.888, 41.664, 72.953, 90.00, 104.78, 90.00
R / Rfree (%) 17.8 / 20

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II (pdb code 2nxs). 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 Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II, PDB code: 2nxs:

Zinc binding site 1 out of 1 in 2nxs

Go back to Zinc Binding Sites List in 2nxs
Zinc binding site 1 out of 1 in the Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural and Kinetic Effects of Hydrophobic Mutations in the Active Site of Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:9.7
occ:1.00
 O2 A:SO4263 1.9 22.5 1.0
NE2 A:HIS96 2.0 7.7 1.0
ND1 A:HIS119 2.0 7.6 1.0
NE2 A:HIS94 2.0 10.6 1.0
CE1 A:HIS119 2.9 8.9 1.0
O3 A:SO4263 2.9 28.1 1.0
CD2 A:HIS96 2.9 8.6 1.0
S A:SO4263 3.0 30.7 1.0
CD2 A:HIS94 3.0 6.7 1.0
CE1 A:HIS96 3.0 9.8 1.0
CE1 A:HIS94 3.1 11.5 1.0
CG A:HIS119 3.1 7.6 1.0
CB A:HIS119 3.6 6.4 1.0
O A:HOH484 3.7 16.6 1.0
OG1 A:THR199 3.9 10.7 1.0
O4 A:SO4263 4.0 28.4 1.0
O1 A:SO4263 4.0 30.8 1.0
OE1 A:GLU106 4.0 11.6 1.0
NE2 A:HIS119 4.1 9.0 1.0
ND1 A:HIS96 4.1 7.7 1.0
CG A:HIS96 4.1 8.1 1.0
CG A:HIS94 4.1 7.3 1.0
ND1 A:HIS94 4.1 6.7 1.0
CD2 A:HIS119 4.2 7.7 1.0
O A:HOH482 4.4 28.2 1.0
CD A:GLU106 4.9 11.5 1.0

Reference:

S.Z.Fisher, C.K.Tu, D.Bhatt, L.Govindasamy, M.Agbandje-Mckenna, R.Mckenna, D.N.Silverman. Speeding Up Proton Transfer in A Fast Enzyme: Kinetic and Crystallographic Studies on the Effect of Hydrophobic Amino Acid Substitutions in the Active Site of Human Carbonic Anhydrase II. Biochemistry V. 46 3803 2007.
ISSN: ISSN 0006-2960
PubMed: 17330962
DOI: 10.1021/BI602620K
Page generated: Thu Oct 17 02:23:00 2024

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