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Zinc in PDB 1cil: The Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors

Enzymatic activity of The Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors

All present enzymatic activity of The Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors:
4.2.1.1;

Protein crystallography data

The structure of The Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors, PDB code: 1cil was solved by G.M.Smith, R.S.Alexander, D.W.Christianson, B.M.Mckeever, G.S.Ponticello, J.P.Springer, W.C.Randall, J.J.Baldwin, C.N.Habecker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.870, 42.130, 72.920, 90.00, 104.55, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the The Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors (pdb code 1cil). 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 Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors, PDB code: 1cil:

Zinc binding site 1 out of 1 in 1cil

Go back to Zinc Binding Sites List in 1cil
Zinc binding site 1 out of 1 in the The Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:5.6
occ:1.00
 N13 A:ETS263 1.9 5.2 1.0
ND1 A:HIS119 2.0 4.2 1.0
NE2 A:HIS94 2.0 5.5 1.0
NE2 A:HIS96 2.1 4.8 1.0
CE1 A:HIS119 2.9 2.9 1.0
CD2 A:HIS94 2.9 5.8 1.0
O11 A:ETS263 2.9 6.8 1.0
CD2 A:HIS96 2.9 6.0 1.0
CE1 A:HIS94 3.0 6.5 1.0
S10 A:ETS263 3.1 5.9 1.0
CG A:HIS119 3.1 4.1 1.0
CE1 A:HIS96 3.1 6.3 1.0
CB A:HIS119 3.5 3.9 1.0
OE1 A:GLU106 4.0 6.4 1.0
OG1 A:THR199 4.0 5.8 1.0
NE2 A:HIS119 4.0 3.9 1.0
CG A:HIS94 4.1 5.6 1.0
ND1 A:HIS94 4.1 5.7 1.0
O12 A:ETS263 4.1 6.3 1.0
C2 A:ETS263 4.1 6.9 1.0
CG A:HIS96 4.1 5.5 1.0
ND1 A:HIS96 4.2 5.9 1.0
CD2 A:HIS119 4.2 4.3 1.0
O A:HOH325 4.4 18.4 1.0
C3 A:ETS263 4.7 7.5 1.0
CD A:GLU106 5.0 6.9 1.0

Reference:

G.M.Smith, R.S.Alexander, D.W.Christianson, B.M.Mckeever, G.S.Ponticello, J.P.Springer, W.C.Randall, J.J.Baldwin, C.N.Habecker. Positions of His-64 and A Bound Water in Human Carbonic Anhydrase II Upon Binding Three Structurally Related Inhibitors. Protein Sci. V. 3 118 1994.
ISSN: ISSN 0961-8368
PubMed: 8142888
Page generated: Sat Oct 12 23:08:33 2024

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