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Mercury in PDB 1fql: X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant

Enzymatic activity of X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant

All present enzymatic activity of X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant:
4.2.1.1;

Protein crystallography data

The structure of X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant, PDB code: 1fql was solved by J.D.Cox, J.A.Hunt, K.M.Compher, C.A.Fierke, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.600, 41.900, 72.700, 90.00, 104.00, 90.00
R / Rfree (%) 17.9 / 25.5

Other elements in 1fql:

The structure of X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant (pdb code 1fql). 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 X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant, PDB code: 1fql:

Mercury binding site 1 out of 1 in 1fql

Go back to Mercury Binding Sites List in 1fql
Mercury binding site 1 out of 1 in the X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:22.4
occ:1.00
 SG A:CYS206 1.9 14.7 1.0
CB A:CYS206 3.1 10.0 1.0
O A:GLN137 3.2 13.1 1.0
O A:GLU205 3.4 9.9 1.0
C A:GLN137 3.5 12.5 1.0
CA A:CYS206 3.5 10.8 1.0
O A:HOH350 3.6 28.1 1.0
C A:GLU205 3.6 11.3 1.0
N A:GLN137 3.7 15.0 1.0
O A:VAL135 3.7 18.9 1.0
N A:CYS206 3.8 11.8 1.0
C A:GLN136 3.9 17.7 1.0
O A:HOH338 4.0 20.6 1.0
C A:VAL135 4.0 16.7 1.0
N A:PRO138 4.1 13.2 1.0
CA A:GLN137 4.1 13.0 1.0
CA A:GLN136 4.3 17.6 1.0
CA A:PRO138 4.3 12.7 1.0
N A:GLN136 4.4 15.4 1.0
O A:GLN136 4.4 17.2 1.0
N A:GLU205 4.5 7.9 1.0
O A:HOH326 4.6 20.0 1.0
CA A:GLU205 4.7 8.2 1.0
CB A:LEU204 4.8 10.6 1.0
CA A:VAL135 4.8 16.4 1.0
O A:ALA134 4.9 18.4 1.0
C A:LEU204 5.0 7.9 1.0
C A:CYS206 5.0 11.8 1.0

Reference:

J.D.Cox, J.A.Hunt, K.M.Compher, C.A.Fierke, D.W.Christianson. Structural Influence of Hydrophobic Core Residues on Metal Binding and Specificity in Carbonic Anhydrase II. Biochemistry V. 39 13687 2000.
ISSN: ISSN 0006-2960
PubMed: 11076507
DOI: 10.1021/BI001649J
Page generated: Sat Aug 10 23:45:10 2024

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