Zinc in PDB 1znc: Human Carbonic Anhydrase IV

All present enzymatic activity of Human Carbonic Anhydrase IV:
4.2.1.1;

The structure of Human Carbonic Anhydrase IV, PDB code: 1znc was solved by T.Stams, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	89.500, 47.700, 141.000, 90.00, 106.30, 90.00
R / Rfree (%)	19.7 / 25.2

The binding sites of Zinc atom in the Human Carbonic Anhydrase IV (pdb code 1znc). 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 IV, PDB code: 1znc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Carbonic Anhydrase IV


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 IV within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:32.0 occ:1.00 ND1 A:HIS119 2.1 10.0 1.0 NE2 A:HIS94 2.2 24.1 1.0 NE2 A:HIS96 2.3 14.6 1.0 O3 A:SO4601 2.4 13.0 1.0 CE1 A:HIS119 2.8 8.4 1.0 CE1 A:HIS94 3.2 23.5 1.0 CD2 A:HIS96 3.2 14.3 1.0 CD2 A:HIS94 3.2 23.4 1.0 CG A:HIS119 3.2 9.6 1.0 CE1 A:HIS96 3.4 12.2 1.0 OG1 A:THR199 3.5 15.3 1.0 HG1 A:THR199 3.6 25.0 1.0 S A:SO4601 3.6 11.5 1.0 CB A:HIS119 3.8 8.4 1.0 O2 A:SO4601 3.9 10.5 1.0 NE2 A:HIS119 4.1 7.7 1.0 OE1 A:GLU106 4.2 16.5 1.0 CD2 A:HIS119 4.3 6.9 1.0 O4 A:SO4601 4.3 13.7 1.0 ND1 A:HIS94 4.3 23.1 1.0 CG A:HIS94 4.4 21.9 1.0 CG A:HIS96 4.5 16.0 1.0 ND1 A:HIS96 4.5 14.2 1.0 O1 A:SO4601 4.6 13.4 1.0 H A:THR199 4.7 25.0 1.0 HE2 A:HIS119 4.9 25.0 1.0 CB A:THR199 4.9 11.6 1.0

Zinc binding site 2 out of 2 in the Human Carbonic Anhydrase IV


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 IV within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:51.7 occ:1.00 ND1 B:HIS119 2.1 16.3 1.0 NE2 B:HIS94 2.3 44.2 1.0 O3 B:SO4701 2.3 33.4 1.0 NE2 B:HIS96 2.4 27.5 1.0 CE1 B:HIS119 2.9 18.1 1.0 CE1 B:HIS94 3.2 43.4 1.0 CD2 B:HIS96 3.3 25.5 1.0 CD2 B:HIS94 3.3 41.1 1.0 CG B:HIS119 3.3 18.4 1.0 OG1 B:THR199 3.4 33.8 1.0 CE1 B:HIS96 3.4 22.9 1.0 HG1 B:THR199 3.6 25.0 1.0 S B:SO4701 3.6 33.5 1.0 CB B:HIS119 3.8 20.6 1.0 O2 B:SO4701 3.9 31.4 1.0 NE2 B:HIS119 4.1 16.0 1.0 OE1 B:GLU106 4.2 26.4 1.0 O4 B:SO4701 4.3 33.4 1.0 CD2 B:HIS119 4.3 18.3 1.0 ND1 B:HIS94 4.4 41.4 1.0 CG B:HIS94 4.4 39.6 1.0 CG B:HIS96 4.5 25.6 1.0 O1 B:SO4701 4.5 32.4 1.0 ND1 B:HIS96 4.5 25.2 1.0 H B:THR199 4.6 25.0 1.0 CB B:THR199 4.9 32.4 1.0 HE2 B:HIS119 4.9 25.0 1.0

T.Stams, S.K.Nair, T.Okuyama, A.Waheed, W.S.Sly, D.W.Christianson. Crystal Structure of the Secretory Form of Membrane-Associated Human Carbonic Anhydrase IV at 2.8-A Resolution. Proc.Natl.Acad.Sci.Usa V. 93 13589 1996.
ISSN: ISSN 0027-8424
PubMed: 8942978
DOI: 10.1073/PNAS.93.24.13589