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Cobalt in PDB 1fqr: X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant

Enzymatic activity of X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant

All present enzymatic activity of X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant:
4.2.1.1;

Protein crystallography data

The structure of X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant, PDB code: 1fqr 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 (°) 42.000, 42.300, 72.400, 90.00, 103.10, 90.00
R / Rfree (%) 21.6 / 27.5

Cobalt Binding Sites:

The binding sites of Cobalt atom in the X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant (pdb code 1fqr). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant, PDB code: 1fqr:

Cobalt binding site 1 out of 1 in 1fqr

Go back to Cobalt Binding Sites List in 1fqr
Cobalt binding site 1 out of 1 in the X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of X-Ray Crystal Structure of Cobalt-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co262

b:23.7
occ:1.00
 O A:HOH301 1.9 15.6 1.0
ND1 A:HIS119 2.0 14.7 1.0
NE2 A:HIS94 2.1 14.1 1.0
NE2 A:HIS96 2.2 14.4 1.0
CE1 A:HIS119 2.8 12.1 1.0
CD2 A:HIS96 3.0 14.6 1.0
CD2 A:HIS94 3.0 15.3 1.0
CG A:HIS119 3.1 13.7 1.0
CE1 A:HIS94 3.2 15.2 1.0
CE1 A:HIS96 3.4 13.3 1.0
CB A:HIS119 3.7 14.2 1.0
OG1 A:THR199 3.8 18.4 1.0
O A:HOH302 3.8 34.9 1.0
OE1 A:GLU106 3.9 10.5 1.0
NE2 A:HIS119 4.0 12.6 1.0
CD2 A:HIS119 4.2 9.1 1.0
CG A:HIS94 4.2 15.7 1.0
CG A:HIS96 4.2 14.6 1.0
ND1 A:HIS94 4.2 17.5 1.0
ND1 A:HIS96 4.4 17.7 1.0
CD A:GLU106 4.7 14.4 1.0
CG2 A:THR199 4.8 13.7 1.0
CB A:THR199 4.9 19.4 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: Tue Jul 30 14:15:48 2024

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