Zinc in PDB 1i6p: Crystal Structure of E. Coli Beta Carbonic Anhydrase (Ecca)

All present enzymatic activity of Crystal Structure of E. Coli Beta Carbonic Anhydrase (Ecca):
4.2.1.1;

The structure of Crystal Structure of E. Coli Beta Carbonic Anhydrase (Ecca), PDB code: 1i6p was solved by J.D.Cronk, J.A.Endrizzi, M.R.Cronk, J.W.O'neill, K.Y.J.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.21 / 2.00
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.535, 68.535, 85.877, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 20.2

The binding sites of Zinc atom in the Crystal Structure of E. Coli Beta Carbonic Anhydrase (Ecca) (pdb code 1i6p). 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 Crystal Structure of E. Coli Beta Carbonic Anhydrase (Ecca), PDB code: 1i6p:

Zinc binding site 1 out of 1 in the Crystal Structure of E. Coli Beta Carbonic Anhydrase (Ecca)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of E. Coli Beta Carbonic Anhydrase (Ecca) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:20.3 occ:1.00 OD2 A:ASP44 2.1 15.6 1.0 NE2 A:HIS98 2.2 15.7 1.0 SG A:CYS42 2.3 16.7 1.0 SG A:CYS101 2.4 18.8 1.0 CG A:ASP44 3.0 19.2 1.0 CD2 A:HIS98 3.1 15.2 1.0 CE1 A:HIS98 3.2 16.7 1.0 CB A:CYS42 3.2 17.2 1.0 CB A:CYS101 3.3 17.0 1.0 CB A:ASP44 3.4 17.9 1.0 CA A:CYS101 3.7 18.8 1.0 N A:GLY102 4.1 19.1 1.0 OD1 A:ASP44 4.2 19.5 1.0 O A:HOH307 4.3 17.8 1.0 ND1 A:HIS98 4.3 16.3 1.0 CG A:HIS98 4.3 16.8 1.0 C A:CYS101 4.3 18.4 1.0 N A:ASP44 4.4 16.5 1.0 CA A:ASP44 4.5 18.8 1.0 CA A:CYS42 4.7 16.7 1.0 N A:ALA67 4.7 14.5 1.0 N A:GLY103 4.7 18.1 1.0 CA A:ALA67 4.7 15.0 1.0 O A:HOH356 4.9 38.2 1.0 N A:CYS101 5.0 20.6 1.0

J.D.Cronk, J.A.Endrizzi, M.R.Cronk, J.W.O'neill, K.Y.Zhang. Crystal Structure of E. Coli Beta-Carbonic Anhydrase, An Enzyme with An Unusual pH-Dependent Activity. Protein Sci. V. 10 911 2001.
ISSN: ISSN 0961-8368
PubMed: 11316870
DOI: 10.1110/PS.46301