Zinc in PDB 6uzu: Carbonic Anhydrase IX-Mimic in Complex with U-CH3

All present enzymatic activity of Carbonic Anhydrase IX-Mimic in Complex with U-CH3:
4.2.1.1;

The structure of Carbonic Anhydrase IX-Mimic in Complex with U-CH3, PDB code: 6uzu was solved by R.Mckenna, M.Y.Mboge, B.P.Mahon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.09 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.152, 41.364, 71.933, 90.00, 103.83, 90.00
R / Rfree (%)	16.1 / 18.4

The binding sites of Zinc atom in the Carbonic Anhydrase IX-Mimic in Complex with U-CH3 (pdb code 6uzu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Carbonic Anhydrase IX-Mimic in Complex with U-CH3, PDB code: 6uzu:

Zinc binding site 1 out of 1 in the Carbonic Anhydrase IX-Mimic in Complex with U-CH3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carbonic Anhydrase IX-Mimic in Complex with U-CH3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:9.2 occ:1.00 NAV A:6LU302 1.9 10.6 1.0 NE2 A:HIS94 2.0 8.1 1.0 ND1 A:HIS119 2.0 7.7 1.0 NE2 A:HIS96 2.0 7.4 1.0 CE1 A:HIS119 2.9 7.2 1.0 CD2 A:HIS94 3.0 8.9 1.0 CD2 A:HIS96 3.0 8.5 1.0 CE1 A:HIS94 3.0 9.2 1.0 OAU A:6LU302 3.0 7.4 1.0 SAQ A:6LU302 3.0 9.8 1.0 CE1 A:HIS96 3.1 8.3 1.0 CG A:HIS119 3.1 7.4 1.0 CB A:HIS119 3.6 6.0 1.0 O A:HOH522 3.7 13.2 1.0 OG1 A:THR199 3.8 8.5 1.0 OE1 A:GLU106 4.0 9.1 1.0 NE2 A:HIS119 4.1 9.5 1.0 ND1 A:HIS94 4.1 9.6 1.0 CG A:HIS94 4.1 8.4 1.0 OAT A:6LU302 4.1 8.5 1.0 CG A:HIS96 4.2 9.7 1.0 ND1 A:HIS96 4.2 9.7 1.0 CD2 A:HIS119 4.2 8.7 1.0 CAC A:6LU302 4.3 9.3 1.0 CD A:GLU106 4.9 11.2 1.0 CAD A:6LU302 4.9 10.5 1.0 O A:HOH474 5.0 17.7 1.0

M.Y.Mboge, B.P.Mahon, N.Lamas, L.Socorro, F.Carta, C.T.Supuran, S.C.Frost, R.Mckenna. Structure Activity Study of Carbonic Anhydrase IX: Selective Inhibition with Ureido-Substituted Benzenesulfonamides. Eur J Med Chem V. 132 184 2017.
ISSN: ISSN 1768-3254
DOI: 10.1016/J.EJMECH.2017.03.026