Zinc in PDB 4cac: Refined Structure of Human Carbonic Anhydrase II at 2.0 Angstroms Resolution

All present enzymatic activity of Refined Structure of Human Carbonic Anhydrase II at 2.0 Angstroms Resolution:
4.2.1.1;

The structure of Refined Structure of Human Carbonic Anhydrase II at 2.0 Angstroms Resolution, PDB code: 4cac was solved by M.Lindahl, D.Habash, S.Harrop, D.R.Helliwell, A.Liljas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Refined Structure of Human Carbonic Anhydrase II at 2.0 Angstroms Resolution (pdb code 4cac). 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 Refined Structure of Human Carbonic Anhydrase II at 2.0 Angstroms Resolution, PDB code: 4cac:

Zinc binding site 1 out of 1 in the Refined Structure of Human Carbonic Anhydrase II at 2.0 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Refined Structure of Human Carbonic Anhydrase II at 2.0 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:8.2 occ:1.00 O A:HOH263 1.8 0.0 1.0 NE2 A:HIS94 2.1 7.2 1.0 NE2 A:HIS96 2.1 3.9 1.0 ND1 A:HIS119 2.2 3.0 1.0 CD2 A:HIS94 3.0 7.3 1.0 CD2 A:HIS96 3.0 4.0 1.0 CE1 A:HIS119 3.0 3.9 1.0 CE1 A:HIS94 3.1 7.8 1.0 CE1 A:HIS96 3.2 4.2 1.0 CG A:HIS119 3.2 3.6 1.0 CB A:HIS119 3.7 3.0 1.0 OG1 A:THR199 3.8 5.6 1.0 O A:HOH317 3.9 19.2 1.0 OE1 A:GLU106 4.0 6.7 1.0 O A:HOH337 4.1 20.4 1.0 ND1 A:HIS94 4.2 7.1 1.0 CG A:HIS94 4.2 6.6 1.0 NE2 A:HIS119 4.2 3.2 1.0 CG A:HIS96 4.2 3.6 1.0 ND1 A:HIS96 4.3 4.3 1.0 CD2 A:HIS119 4.3 3.5 1.0 CD A:GLU106 4.8 6.9 1.0

A.E.Eriksson, T.A.Jones, A.Liljas. Refined Structure of Human Carbonic Anhydrase II at 2.0 A Resolution. Proteins V. 4 274 1988.
ISSN: ISSN 0887-3585
PubMed: 3151019
DOI: 10.1002/PROT.340040406