Copper in PDB 6skt: Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0)

All present enzymatic activity of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0):
4.2.1.1;

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0), PDB code: 6skt was solved by M.R.Groves, W.Wang, N.Van Oosterwijk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.40 / 1.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	67.619, 67.619, 123.429, 90.00, 90.00, 120.00
R / Rfree (%)	17.7 / 20.4

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Copper atom in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0) (pdb code 6skt). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0), PDB code: 6skt:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:42.7 occ:1.00 ND1 A:HIS4 2.1 53.6 1.0 NE2 A:HIS15 2.1 39.7 1.0 OD2 A:ASP19 2.2 52.2 1.0 O A:HIS4 2.5 49.5 1.0 CE1 A:HIS15 3.0 39.5 1.0 CE1 A:HIS4 3.1 54.2 1.0 CG A:ASP19 3.1 52.4 1.0 CG A:HIS4 3.1 55.1 1.0 OD1 A:ASP19 3.2 54.2 1.0 CD2 A:HIS15 3.2 39.9 1.0 CB A:HIS4 3.4 55.0 1.0 C A:HIS4 3.5 51.4 1.0 CA A:HIS4 4.0 54.9 1.0 NE2 A:HIS4 4.2 56.0 1.0 ND1 A:HIS15 4.2 38.6 1.0 CD2 A:HIS4 4.2 55.6 1.0 CG A:HIS15 4.3 38.7 1.0 N A:TRP5 4.5 47.5 1.0 CB A:ASP19 4.5 49.5 1.0 CA A:TRP5 4.9 45.1 1.0 N A:HIS4 5.0 59.8 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1005 b:65.8 occ:1.00 NE2 A:HIS3 2.3 67.1 1.0 NE2 A:HIS64 2.4 55.2 1.0 O A:TRP5 2.5 43.5 1.0 O A:HOH1130 2.8 48.9 1.0 CD2 A:HIS64 2.9 53.4 1.0 CE1 A:HIS3 3.2 66.4 1.0 CD2 A:HIS3 3.3 67.9 1.0 CE1 A:HIS64 3.6 54.7 1.0 C A:TRP5 3.6 43.0 1.0 CA A:GLY6 3.9 38.6 1.0 O A:GLY63 4.2 39.6 1.0 CG A:HIS64 4.2 49.6 1.0 N A:GLY6 4.2 40.1 1.0 ND1 A:HIS3 4.3 69.0 1.0 CG A:HIS3 4.4 69.3 1.0 ND1 A:HIS64 4.5 53.0 1.0 ND2 A:ASN11 4.5 41.3 1.0 O A:HOH1226 4.5 46.8 1.0 CA A:TRP5 4.8 45.1 1.0 N A:TRP5 4.9 47.5 1.0 CD2 A:TRP5 5.0 42.0 1.0

M.R.Groves, W.Wang, N.Van Oosterwijk, M.Witte, J.Lohse. Target Diazotransfer Reagents to Label Metalloenzymes To Be Published.