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Zinc in PDB 1caj: Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II

Enzymatic activity of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II

All present enzymatic activity of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II, PDB code: 1caj was solved by Y.Xue, A.Liljas, B.-H.Jonsson, S.Lindskog, 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 Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II (pdb code 1caj). 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 Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II, PDB code: 1caj:

Zinc binding site 1 out of 1 in 1caj

Go back to Zinc Binding Sites List in 1caj
Zinc binding site 1 out of 1 in the Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network 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 Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:10.2
occ:1.00
 ND1 A:HIS119 2.1 7.8 1.0
NE2 A:HIS94 2.2 7.2 1.0
O A:HOH263 2.2 10.2 0.6
O2 A:SO4500 2.2 20.5 0.4
NE2 A:HIS96 2.2 4.3 1.0
O4 A:SO4500 2.9 20.6 0.4
CE1 A:HIS119 3.0 6.2 1.0
CD2 A:HIS94 3.0 7.0 1.0
S A:SO4500 3.0 20.9 0.4
CG A:HIS119 3.1 6.9 1.0
CE1 A:HIS96 3.1 3.4 1.0
CD2 A:HIS96 3.1 3.7 1.0
CE1 A:HIS94 3.2 5.8 1.0
CB A:HIS119 3.5 5.3 1.0
O A:HOH318 3.7 32.8 1.0
O3 A:SO4500 3.9 20.2 0.4
OG1 A:THR199 4.0 5.7 1.0
NE2 A:HIS119 4.1 5.0 1.0
O1 A:SO4500 4.1 20.5 0.4
CD2 A:HIS119 4.2 5.7 1.0
CG A:HIS94 4.2 5.5 1.0
ND1 A:HIS96 4.2 5.0 1.0
ND1 A:HIS94 4.2 6.3 1.0
CG A:HIS96 4.2 3.2 1.0
OD2 A:ASP106 4.3 9.8 1.0
O A:HOH292 4.4 22.7 1.0
CA A:HIS119 5.0 5.2 1.0

Reference:

Y.Xue, A.Liljas, B.H.Jonsson, S.Lindskog. Structural Analysis of the Zinc Hydroxide-Thr-199-Glu-106 Hydrogen-Bond Network in Human Carbonic Anhydrase II. Proteins V. 17 93 1993.
ISSN: ISSN 0887-3585
PubMed: 7901850
DOI: 10.1002/PROT.340170112
Page generated: Sat Oct 12 22:59:58 2024

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