Copper in PDB 2fos: Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors

All present enzymatic activity of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors:
4.2.1.1;

The structure of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors, PDB code: 2fos was solved by K.M.Jude, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	80.00 / 1.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.444, 41.640, 72.278, 90.00, 104.24, 90.00
R / Rfree (%)	12.7 / 15.3

The structure of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors also contains other interesting chemical elements:

Mercury	(Hg)	1 atom
Zinc	(Zn)	1 atom

The binding sites of Copper atom in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors (pdb code 2fos). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors, PDB code: 2fos:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:44.0 occ:0.74 NE2 A:HIS64 2.4 27.9 0.7 CD2 A:HIS64 3.2 21.1 0.7 CE1 A:HIS64 3.5 25.8 0.7 CD2 A:HIS64 3.9 14.4 0.3 O A:HOH687 3.9 37.2 1.0 NE2 A:HIS64 4.0 15.9 0.3 O A:ASN62 4.3 12.9 1.0 CG A:HIS64 4.4 17.5 0.7 ND1 A:HIS64 4.5 22.1 0.7 NE1 A:TRP5 4.6 16.9 1.0 CZ2 A:TRP5 4.7 15.2 1.0 CE2 A:TRP5 4.8 13.7 1.0 O A:HOH662 5.0 33.8 0.5

Copper binding site 2 out of 2 in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu304 b:34.0 occ:0.75 ND1 A:HIS3 1.9 33.0 1.0 CA A:SER2 2.0 36.8 0.3 N A:HIS3 2.2 40.7 1.0 C A:SER2 2.4 37.0 0.3 CE1 A:HIS3 2.7 40.7 1.0 OG A:SER2 2.7 38.0 0.3 CB A:SER2 2.8 34.1 0.3 N A:SER2 3.1 47.4 0.3 CG A:HIS3 3.1 36.5 1.0 CA A:HIS3 3.4 34.4 1.0 O A:HIS3 3.6 26.9 1.0 O A:SER2 3.7 29.8 0.3 CB A:HIS3 3.7 38.4 1.0 O A:HOH547 3.7 35.9 1.0 NE2 A:HIS3 3.9 41.8 1.0 C A:HIS3 4.0 26.0 1.0 CD2 A:HIS3 4.1 37.3 1.0

K.M.Jude, A.L.Banerjee, M.K.Haldar, S.Manokaran, B.Roy, S.Mallik, D.K.Srivastava, D.W.Christianson. Ultrahigh Resolution Crystal Structures of Human Carbonic Anhydrases I and II Complexed with Two-Prong Inhibitors Reveal the Molecular Basis of High Affinity. J.Am.Chem.Soc. V. 128 3011 2006.
ISSN: ISSN 0002-7863
PubMed: 16506782
DOI: 10.1021/JA057257N