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Zinc 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:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the X-Ray Crystal Structure of Zinc-Bound F95M/W97V Carbonic Anhydrase (Caii) Variant, PDB code: 1fql:

Zinc binding site 1 out of 1 in 1fql

Go back to Zinc Binding Sites List in 1fql
Zinc 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 Zinc with other atoms in the Zn 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:Zn262

b:10.4
occ:1.00
 O A:HOH310 1.9 20.6 1.0
NE2 A:HIS94 1.9 4.9 1.0
ND1 A:HIS119 2.0 8.9 1.0
NE2 A:HIS96 2.0 6.9 1.0
CE1 A:HIS119 2.9 6.0 1.0
CD2 A:HIS94 2.9 3.4 1.0
CE1 A:HIS96 3.0 3.3 1.0
CE1 A:HIS94 3.0 2.9 1.0
CD2 A:HIS96 3.1 2.4 1.0
CG A:HIS119 3.1 7.6 1.0
CB A:HIS119 3.6 7.5 1.0
O A:HOH314 3.8 19.7 1.0
OG1 A:THR199 3.8 7.3 1.0
O A:HOH309 3.9 20.6 1.0
OE1 A:GLU106 4.0 6.5 1.0
NE2 A:HIS119 4.0 6.3 1.0
CG A:HIS94 4.1 5.3 1.0
ND1 A:HIS94 4.1 6.1 1.0
ND1 A:HIS96 4.1 4.6 1.0
CD2 A:HIS119 4.2 6.8 1.0
CG A:HIS96 4.2 4.7 1.0
CD A:GLU106 4.9 8.5 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: Wed Dec 16 02:49:35 2020

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