Zinc in PDB 1ttm: Human Carbonic Anhydrase II Complexed with 667-Coumate

All present enzymatic activity of Human Carbonic Anhydrase II Complexed with 667-Coumate:
4.2.1.1;

The structure of Human Carbonic Anhydrase II Complexed with 667-Coumate, PDB code: 1ttm was solved by M.D.Lloyd, R.L.Pederick, R.Natesh, L.W.L.Woo, A.Purohit, M.J.Reed, K.R.Acharya, B.V.L.Potter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.24 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.525, 72.522, 75.379, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 21

The binding sites of Zinc atom in the Human Carbonic Anhydrase II Complexed with 667-Coumate (pdb code 1ttm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Carbonic Anhydrase II Complexed with 667-Coumate, PDB code: 1ttm:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Carbonic Anhydrase II Complexed with 667-Coumate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II Complexed with 667-Coumate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:9.5 occ:1.00 ND1 A:HIS119 2.1 8.8 1.0 N1 A:667264 2.1 22.6 1.0 NE2 A:HIS94 2.1 13.2 1.0 NE2 A:HIS96 2.2 6.8 1.0 CD2 A:HIS96 3.0 7.1 1.0 CE1 A:HIS119 3.0 12.0 1.0 S1 A:667264 3.0 20.3 1.0 CD2 A:HIS94 3.0 11.0 1.0 CE1 A:HIS94 3.2 10.6 1.0 CG A:HIS119 3.2 11.1 1.0 O2 A:667264 3.2 20.9 1.0 CE1 A:HIS96 3.3 5.6 1.0 O3 A:667264 3.4 23.9 1.0 CB A:HIS119 3.6 9.5 1.0 OG1 A:THR199 4.0 8.1 1.0 OE1 A:GLU106 4.0 8.9 1.0 NE2 A:HIS119 4.2 11.9 1.0 CG A:HIS94 4.2 10.9 1.0 CG A:HIS96 4.2 6.7 1.0 ND1 A:HIS94 4.2 10.1 1.0 CD2 A:HIS119 4.3 8.3 1.0 O A:HOH355 4.3 26.2 1.0 ND1 A:HIS96 4.3 7.0 1.0 O1 A:667264 4.6 24.7 1.0 C1 A:667264 4.7 29.4 1.0 CD A:GLU106 5.0 8.4 1.0

Zinc binding site 2 out of 2 in the Human Carbonic Anhydrase II Complexed with 667-Coumate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Carbonic Anhydrase II Complexed with 667-Coumate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn263 b:24.8 occ:1.00 O A:HOH429 2.1 22.6 1.0 ND1 A:HIS36 2.3 23.6 1.0 O A:HOH285 2.4 48.5 1.0 CG A:HIS36 3.2 22.8 1.0 CE1 A:HIS36 3.3 25.4 1.0 CB A:HIS36 3.5 22.7 1.0 CA A:HIS36 4.1 22.2 1.0 NE2 A:HIS36 4.3 25.1 1.0 CD2 A:HIS36 4.3 24.8 1.0 O A:HIS36 4.7 26.0 1.0 C A:HIS36 4.9 22.8 1.0

M.D.Lloyd, R.L.Pederick, R.Natesh, L.W.L.Woo, A.Purohit, M.J.Reed, K.R.Acharya, B.V.L.Potter. Crystal Structure of Human Carbonic Anhydrase II at 1.95 A Resolution in Complex with 667-Coumate, A Novel Anti-Cancer Agent Biochem.J. V. 385 715 2005.
ISSN: ISSN 0264-6021
PubMed: 15453828
DOI: 10.1042/BJ20041037