Copper in PDB 6lva: Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2

All present enzymatic activity of Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2:
4.2.1.1;

The structure of Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2, PDB code: 6lva was solved by C.U.Kim, J.K.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.359, 41.402, 72.307, 90.00, 103.97, 90.00
R / Rfree (%)	11.3 / 14.2

The binding sites of Copper atom in the Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2 (pdb code 6lva). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2, PDB code: 6lva:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:5.8 occ:1.00 HD1 A:HIS119 1.2 4.1 1.0 HE2 A:HIS96 1.2 5.0 1.0 HE2 A:HIS94 1.2 3.9 1.0 ND1 A:HIS119 2.0 4.4 1.0 NE2 A:HIS94 2.0 4.5 1.0 NE2 A:HIS96 2.0 5.0 1.0 O A:HOH421 2.3 19.4 1.0 CE1 A:HIS119 2.9 4.0 1.0 CD2 A:HIS94 3.0 4.6 1.0 CD2 A:HIS96 3.0 4.4 1.0 CE1 A:HIS94 3.0 4.7 1.0 CG A:HIS119 3.0 4.4 1.0 HE1 A:HIS119 3.0 3.9 1.0 HB2 A:HIS119 3.1 4.4 1.0 CE1 A:HIS96 3.1 5.7 1.0 O A:HOH675 3.1 36.6 1.0 HD2 A:HIS94 3.1 4.4 1.0 HD2 A:HIS96 3.2 4.5 1.0 HE1 A:HIS94 3.2 4.7 1.0 HE1 A:HIS96 3.3 5.9 1.0 CB A:HIS119 3.5 4.3 1.0 HG1 A:THR199 3.6 5.5 0.0 HB3 A:HIS119 3.7 4.2 1.0 O A:HOH695 3.8 36.3 1.0 OG1 A:THR199 3.9 5.6 1.0 NE2 A:HIS119 4.0 4.1 1.0 O A:HOH697 4.1 29.2 1.0 ND1 A:HIS94 4.1 4.5 1.0 CG A:HIS94 4.1 4.1 1.0 CD2 A:HIS119 4.2 4.5 1.0 OE1 A:GLU106 4.2 4.8 1.0 ND1 A:HIS96 4.2 6.2 1.0 O A:HOH496 4.2 28.1 1.0 CG A:HIS96 4.2 4.7 1.0 HH2 A:TRP209 4.4 5.7 1.0 O A:HOH681 4.6 17.6 1.0 O A:HOH427 4.7 27.8 1.0 HE2 A:HIS119 4.8 3.5 1.0 HD1 A:HIS94 4.9 3.7 1.0 CA A:HIS119 4.9 4.0 1.0 HD1 A:HIS96 5.0 5.4 1.0 HG23 A:THR200 5.0 8.8 1.0 H A:THR199 5.0 4.6 1.0

Copper binding site 2 out of 2 in the Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu- Carbonic Anhydrase II pH 7.8 20 Atm CO2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu304 b:27.3 occ:1.00 HD2 A:HIS4 1.4 32.9 1.0 H A:HIS4 1.4 21.2 1.0 N A:HIS4 1.8 23.5 1.0 CD2 A:HIS4 2.1 39.2 1.0 CG A:HIS4 2.9 29.2 1.0 CA A:HIS4 3.0 17.7 1.0 H A:TRP5 3.0 19.1 1.0 O A:HOH573 3.2 25.8 1.0 CB A:HIS4 3.2 26.4 1.0 NE2 A:HIS4 3.3 75.3 1.0 HB3 A:HIS4 3.3 19.7 1.0 HE2 A:HIS4 3.6 69.7 1.0 HA A:HIS4 3.6 19.3 1.0 N A:TRP5 3.7 17.7 1.0 C A:HIS4 3.9 30.1 1.0 ND1 A:HIS4 4.1 59.2 1.0 HB2 A:HIS4 4.2 25.5 1.0 CE1 A:HIS4 4.3 52.6 1.0 O A:TRP5 4.6 12.4 1.0 HD1 A:TRP5 4.7 11.4 1.0 HD1 A:HIS4 4.9 57.3 1.0 O A:HOH693 4.9 53.7 1.0 CA A:TRP5 5.0 11.7 1.0

C.U.Kim, J.K.Kim. Metal Substituted Human Carbonic Anhydrase II Under CO2 Pressure To Be Published.