Copper in PDB 2fou: 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: 2fou 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)	60.00 / 0.99
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.557, 41.704, 72.710, 90.00, 104.38, 90.00
R / Rfree (%)	12.3 / 13.5

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 2fou). 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: 2fou:
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:Cu302 b:19.4 occ:0.52 ND1 A:HIS3 1.9 25.3 1.0 N A:HIS3 2.0 29.2 1.0 OG A:SER2 2.2 52.8 1.0 CG A:HIS3 2.8 25.7 1.0 C A:SER2 2.9 32.7 1.0 CE1 A:HIS3 3.0 24.5 1.0 CA A:SER2 3.0 48.3 1.0 CA A:HIS3 3.0 23.6 1.0 CB A:SER2 3.0 52.1 1.0 CB A:HIS3 3.1 25.9 1.0 O A:HIS3 3.6 20.4 1.0 C A:HIS3 3.7 20.2 1.0 O A:HOH602 3.7 19.3 0.5 CD2 A:HIS3 4.0 27.3 1.0 NE2 A:HIS3 4.0 27.4 1.0 O A:SER2 4.0 34.5 1.0 N A:SER2 4.4 47.4 1.0 O A:HOH641 4.9 45.4 0.5 N A:HIS4 5.0 20.4 1.0

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:Cu303 b:55.3 occ:0.82 CU A:B22303 0.0 55.3 0.8 C23 A:B22303 1.7 68.0 0.8 NE2 A:HIS4 1.8 35.6 1.0 OXD A:B22303 2.0 69.3 0.8 OXB A:B22303 2.0 57.2 0.8 C24 A:B22303 2.1 68.6 0.8 N20 A:B22303 2.1 64.2 0.8 N17 A:B22303 2.4 56.3 0.8 CE1 A:HIS4 2.8 36.1 1.0 C22 A:B22303 2.8 63.3 0.8 C21 A:B22303 2.8 64.6 0.8 C19 A:B22303 2.9 61.4 0.8 CD2 A:HIS4 2.9 30.1 1.0 C18 A:B22303 2.9 57.7 0.8 C15 A:B22303 3.1 48.1 0.8 OXC A:B22303 3.3 77.9 0.8 C14 A:B22303 3.7 46.7 0.8 C16 A:B22303 3.8 40.6 0.8 ND1 A:HIS4 3.9 28.3 1.0 O18 A:B22303 4.0 66.2 0.8 CG A:HIS4 4.0 23.1 1.0 OXA A:B22303 4.0 63.1 0.8 C13 A:B22303 4.8 42.1 0.8 C11 A:B22303 4.9 37.3 0.8

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