Zinc in PDB 1fr7: X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant

All present enzymatic activity of X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant:
4.2.1.1;

The structure of X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant, PDB code: 1fr7 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 / 1.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	42.240, 43.750, 66.690, 86.86, 89.91, 75.90
R / Rfree (%)	24 / 26

The binding sites of Zinc atom in the X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant (pdb code 1fr7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant, PDB code: 1fr7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M 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 F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:17.5 occ:1.00 O A:HOH301 2.1 40.2 1.0 NE2 A:HIS96 2.1 6.1 1.0 ND1 A:HIS119 2.2 5.9 1.0 NE2 A:HIS94 2.2 17.4 1.0 CD2 A:HIS94 2.6 16.0 1.0 O A:HOH507 2.8 24.4 1.0 CE1 A:HIS119 3.0 6.2 1.0 CD2 A:HIS96 3.0 6.9 1.0 CE1 A:HIS96 3.2 6.0 1.0 CG A:HIS119 3.3 5.0 1.0 CE1 A:HIS94 3.5 16.8 1.0 CB A:HIS119 3.8 5.5 1.0 OG1 A:THR199 3.8 8.2 1.0 CG A:HIS94 3.9 11.3 1.0 OE1 A:GLU106 3.9 8.6 1.0 NE2 A:HIS119 4.2 6.8 1.0 CG A:HIS96 4.2 7.0 1.0 ND1 A:HIS96 4.3 6.1 1.0 ND1 A:HIS94 4.3 12.9 1.0 CD2 A:HIS119 4.4 6.9 1.0 CD A:GLU106 4.8 7.4 1.0

Zinc binding site 2 out of 2 in the X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Crystal Structure of Zinc-Bound F93S/F95L/W97M Carbonic Anhydrase (Caii) Variant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn263 b:17.5 occ:1.00 O B:HOH550 2.1 40.2 1.0 NE2 B:HIS96 2.1 6.1 1.0 ND1 B:HIS119 2.2 5.9 1.0 NE2 B:HIS94 2.2 17.4 1.0 CD2 B:HIS94 2.6 16.0 1.0 O B:HOH753 2.8 24.4 1.0 CE1 B:HIS119 3.0 6.2 1.0 CD2 B:HIS96 3.0 6.9 1.0 CE1 B:HIS96 3.2 6.0 1.0 CG B:HIS119 3.3 5.0 1.0 CE1 B:HIS94 3.5 16.8 1.0 CB B:HIS119 3.8 5.5 1.0 OG1 B:THR199 3.8 8.2 1.0 CG B:HIS94 3.9 11.3 1.0 OE1 B:GLU106 3.9 8.6 1.0 NE2 B:HIS119 4.2 6.8 1.0 CG B:HIS96 4.2 7.0 1.0 ND1 B:HIS96 4.3 6.1 1.0 ND1 B:HIS94 4.3 12.9 1.0 CD2 B:HIS119 4.4 6.9 1.0 CD B:GLU106 4.8 7.4 1.0

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