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Mercury in PDB 2ca2: Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H

Enzymatic activity of Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H

All present enzymatic activity of Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H:
4.2.1.1;

Protein crystallography data

The structure of Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H, PDB code: 2ca2 was solved by A.E.Eriksson, P.M.Kylsten, T.A.Jones, A.Liljas, 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

Other elements in 2ca2:

The structure of Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H (pdb code 2ca2). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H, PDB code: 2ca2:

Mercury binding site 1 out of 1 in 2ca2

Go back to Mercury Binding Sites List in 2ca2
Mercury binding site 1 out of 1 in the Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II. A Pentacoordinated Binding of the Scn-Ion to the Zinc at High P*H within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg262

b:36.1
occ:1.00
SG A:CYS206 2.3 23.1 1.0
CB A:CYS206 3.1 18.8 1.0
O A:GLN137 3.2 16.9 1.0
O A:GLU205 3.3 14.5 1.0
CA A:CYS206 3.4 16.4 1.0
C A:GLN137 3.5 18.0 1.0
C A:GLU205 3.5 15.4 1.0
O A:VAL135 3.6 19.3 1.0
N A:CYS206 3.6 16.2 1.0
N A:GLN137 3.7 18.6 1.0
O A:HOH333 3.8 20.9 1.0
C A:GLN136 3.9 19.6 1.0
N A:PRO138 4.0 17.5 1.0
CA A:GLN137 4.1 18.5 1.0
C A:VAL135 4.2 19.1 1.0
CA A:GLN136 4.3 20.1 1.0
N A:GLU205 4.3 15.5 1.0
CA A:PRO138 4.3 17.6 1.0
O A:GLN136 4.3 18.8 1.0
CA A:GLU205 4.4 15.6 1.0
N A:GLN136 4.5 19.2 1.0
CB A:LEU204 4.6 15.8 1.0
C A:LEU204 4.8 15.1 1.0
C A:CYS206 4.9 15.1 1.0
CD A:PRO138 5.0 17.7 1.0

Reference:

A.E.Eriksson, P.M.Kylsten, T.A.Jones, A.Liljas. Crystallographic Studies of Inhibitor Binding Sites in Human Carbonic Anhydrase II: A Pentacoordinated Binding of the Scn- Ion to the Zinc at High pH. Proteins V. 4 283 1988.
ISSN: ISSN 0887-3585
PubMed: 3151020
DOI: 10.1002/PROT.340040407
Page generated: Wed Oct 28 18:41:17 2020

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