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Zinc in PDB 1th9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

Enzymatic activity of Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

All present enzymatic activity of Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II, PDB code: 1th9 was solved by Z.Fisher, J.A.Hernandez Prada, C.K.Tu, D.Duda, C.Yoshioka, H.An, L.Govindasamy, D.N.Silverman, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.63
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.616, 41.505, 72.872, 90.00, 104.63, 90.00
R / Rfree (%) 17.7 / 21.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II (pdb code 1th9). 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 Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II, PDB code: 1th9:

Zinc binding site 1 out of 1 in 1th9

Go back to Zinc Binding Sites List in 1th9
Zinc binding site 1 out of 1 in the Effect of Shuttle Location and pH Environment on H+ Transfer 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 Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:10.7
occ:1.00
 O2 A:SO4263 2.0 27.8 1.0
NE2 A:HIS94 2.0 9.5 1.0
ND1 A:HIS119 2.0 8.1 1.0
NE2 A:HIS96 2.1 9.1 1.0
CE1 A:HIS119 2.9 7.2 1.0
CD2 A:HIS94 3.0 11.3 1.0
CE1 A:HIS94 3.0 11.7 1.0
CD2 A:HIS96 3.0 8.8 1.0
S A:SO4263 3.0 37.4 1.0
O3 A:SO4263 3.0 35.6 1.0
CE1 A:HIS96 3.1 10.5 1.0
CG A:HIS119 3.1 7.2 1.0
CB A:HIS119 3.6 7.6 1.0
O A:HOH410 3.8 34.9 1.0
OG1 A:THR199 3.8 11.0 1.0
O4 A:SO4263 3.9 34.9 1.0
OE1 A:GLU106 4.0 11.3 1.0
NE2 A:HIS119 4.0 6.5 1.0
ND1 A:HIS94 4.1 9.8 1.0
CG A:HIS94 4.1 8.6 1.0
ND1 A:HIS96 4.1 9.8 1.0
O1 A:SO4263 4.1 34.6 1.0
CG A:HIS96 4.2 7.5 1.0
CD2 A:HIS119 4.2 8.6 1.0
O A:HOH382 4.9 37.3 1.0
CD A:GLU106 4.9 12.0 1.0
O A:HOH302 4.9 33.1 1.0

Reference:

Z.Fisher, J.A.Hernandez Prada, C.K.Tu, D.Duda, C.Yoshioka, H.An, L.Govindasamy, D.N.Silverman, R.Mckenna. Structural and Kinetic Characterization of Active-Site Histidine As A Proton Shuttle in Catalysis By Human Carbonic Anhydrase II Biochemistry V. 44 1097 2005.
ISSN: ISSN 0006-2960
PubMed: 15667203
DOI: 10.1021/BI0480279
Page generated: Tue Aug 19 23:20:56 2025

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