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Copper in PDB 1fr4: X-Ray Crystal Structure of Copper-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant

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

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

Protein crystallography data

The structure of X-Ray Crystal Structure of Copper-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant, PDB code: 1fr4 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 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.000, 41.200, 72.100, 90.00, 103.10, 90.00
R / Rfree (%) 22.1 / 25.9

Copper Binding Sites:

The binding sites of Copper atom in the X-Ray Crystal Structure of Copper-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant (pdb code 1fr4). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the X-Ray Crystal Structure of Copper-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant, PDB code: 1fr4:

Copper binding site 1 out of 1 in 1fr4

Go back to Copper Binding Sites List in 1fr4
Copper binding site 1 out of 1 in the X-Ray Crystal Structure of Copper-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of X-Ray Crystal Structure of Copper-Bound F93I/F95M/W97V Carbonic Anhydrase (Caii) Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu262

b:14.2
occ:1.00
 NE2 A:HIS96 2.1 10.0 1.0
NE2 A:HIS94 2.1 10.1 1.0
ND1 A:HIS119 2.2 10.3 1.0
O A:HOH309 2.2 23.3 1.0
O4 A:SO4990 2.4 62.2 1.0
CD2 A:HIS96 3.0 11.1 1.0
CD2 A:HIS94 3.1 7.9 1.0
CE1 A:HIS119 3.1 8.0 1.0
CE1 A:HIS94 3.1 10.1 1.0
CE1 A:HIS96 3.2 10.1 1.0
CG A:HIS119 3.2 9.8 1.0
S A:SO4990 3.3 62.8 1.0
O1 A:SO4990 3.5 65.0 1.0
CB A:HIS119 3.5 9.0 1.0
O2 A:SO4990 3.7 64.1 1.0
OG1 A:THR199 3.7 10.2 1.0
OE1 A:GLU106 4.0 9.4 1.0
O A:HOH394 4.1 27.1 1.0
CG A:HIS96 4.2 11.1 1.0
CG A:HIS94 4.2 9.1 1.0
ND1 A:HIS94 4.2 11.3 1.0
NE2 A:HIS119 4.2 8.6 1.0
ND1 A:HIS96 4.2 11.5 1.0
CD2 A:HIS119 4.3 7.4 1.0
O A:HOH370 4.5 32.2 1.0
O3 A:SO4990 4.7 62.5 1.0
CD A:GLU106 4.7 9.9 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: Sun Jul 13 23:40:23 2025

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