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Zinc in PDB 4l5u: The Structural Implications of the Secondary CO2 Binding Pocket in Human Carbonic Anhydrase II

Enzymatic activity of The Structural Implications of the Secondary CO2 Binding Pocket in Human Carbonic Anhydrase II

All present enzymatic activity of The Structural Implications of the Secondary CO2 Binding Pocket in Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of The Structural Implications of the Secondary CO2 Binding Pocket in Human Carbonic Anhydrase II, PDB code: 4l5u was solved by C.D.Boone, S.Gill, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.99 / 2.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.343, 41.433, 72.453, 90.00, 104.27, 90.00
R / Rfree (%) 15.4 / 20.1

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structural Implications of the Secondary CO2 Binding Pocket in Human Carbonic Anhydrase II (pdb code 4l5u). 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 The Structural Implications of the Secondary CO2 Binding Pocket in Human Carbonic Anhydrase II, PDB code: 4l5u:

Zinc binding site 1 out of 1 in 4l5u

Go back to Zinc Binding Sites List in 4l5u
Zinc binding site 1 out of 1 in the The Structural Implications of the Secondary CO2 Binding Pocket in 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 The Structural Implications of the Secondary CO2 Binding Pocket in Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:15.0
occ:1.00
 NE2 A:HIS94 2.0 1.2 1.0
O A:HOH423 2.0 17.0 1.0
ND1 A:HIS119 2.1 1.1 1.0
NE2 A:HIS96 2.1 1.1 1.0
CD2 A:HIS94 2.9 1.2 1.0
CE1 A:HIS119 2.9 1.1 1.0
CE1 A:HIS94 3.0 1.2 1.0
HE1 A:HIS119 3.0 1.3 1.0
CD2 A:HIS96 3.1 1.1 1.0
HD2 A:HIS94 3.1 1.4 1.0
CE1 A:HIS96 3.1 1.4 1.0
CG A:HIS119 3.1 3.8 1.0
HB2 A:HIS119 3.2 1.4 1.0
HD2 A:HIS96 3.2 1.4 1.0
HE1 A:HIS94 3.3 1.4 1.0
HE1 A:HIS96 3.3 1.7 1.0
CB A:HIS119 3.6 1.2 1.0
O A:HOH425 3.6 19.7 1.0
HG1 A:THR199 3.6 1.3 1.0
HB3 A:HIS119 3.8 1.4 1.0
OG1 A:THR199 3.9 1.1 1.0
O A:HOH496 3.9 26.0 1.0
CG A:HIS94 4.1 1.2 1.0
NE2 A:HIS119 4.1 2.0 1.0
OE1 A:GLU106 4.1 2.0 1.0
ND1 A:HIS94 4.1 1.2 1.0
ND1 A:HIS96 4.2 1.9 1.0
CD2 A:HIS119 4.2 1.1 1.0
CG A:HIS96 4.2 5.2 1.0
HH2 A:TRP209 4.3 1.3 1.0
O A:HOH415 4.5 20.9 1.0
HE2 A:HIS119 4.8 2.4 1.0
HG23 A:THR200 4.9 3.8 1.0
HD1 A:HIS94 4.9 1.5 1.0
CD A:GLU106 4.9 1.1 1.0
H A:THR199 5.0 1.3 1.0
HD1 A:HIS96 5.0 2.3 1.0
O A:HOH437 5.0 28.5 1.0

Reference:

C.D.Boone, S.Gill, C.Tu, D.N.Silverman, R.Mckenna. Structural, Catalytic and Stabilizing Consequences of Aromatic Cluster Variants in Human Carbonic Anhydrase II. Arch.Biochem.Biophys. V. 539 31 2013.
ISSN: ISSN 0003-9861
PubMed: 24036123
DOI: 10.1016/J.ABB.2013.09.001
Page generated: Sun Oct 27 01:35:20 2024

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