Zinc in PDB 2bz1: Crystal Structure of Apo E. Coli Gtp Cyclohydrolase II

All present enzymatic activity of Crystal Structure of Apo E. Coli Gtp Cyclohydrolase II:
3.5.4.25;

The structure of Crystal Structure of Apo E. Coli Gtp Cyclohydrolase II, PDB code: 2bz1 was solved by J.Ren, M.Kotaka, M.Lockyer, H.K.Lamb, A.R.Hawkins, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.57 / 1.54
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	71.920, 71.920, 128.630, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 21.2

The binding sites of Zinc atom in the Crystal Structure of Apo E. Coli Gtp Cyclohydrolase II (pdb code 2bz1). 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 Apo E. Coli Gtp Cyclohydrolase II, PDB code: 2bz1:

Zinc binding site 1 out of 1 in the Crystal Structure of Apo E. Coli Gtp Cyclohydrolase II


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 Apo E. Coli Gtp Cyclohydrolase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1174 b:14.8 occ:1.00 O A:HOH2191 2.0 19.0 1.0 SG A:CYS54 2.3 13.5 1.0 SG A:CYS67 2.3 15.1 1.0 SG A:CYS65 2.3 14.6 1.0 CB A:CYS67 3.1 13.9 1.0 CB A:CYS65 3.2 15.9 1.0 CB A:CYS54 3.2 14.4 1.0 N A:CYS67 4.1 13.5 1.0 O A:HOH2088 4.1 14.8 1.0 O4 A:SO41175 4.2 23.4 1.0 NZ A:LYS101 4.2 23.1 1.0 CA A:CYS67 4.2 12.3 1.0 CA A:GLY57 4.5 12.4 1.0 N A:GLY57 4.6 13.8 1.0 CA A:CYS65 4.7 17.5 1.0 CA A:CYS54 4.7 12.2 1.0 O A:HOH2104 4.7 53.1 1.0 OH A:TYR105 4.7 19.1 1.0 O A:HOH2086 4.8 19.0 1.0 OG1 A:THR56 4.9 13.5 1.0 C A:CYS65 5.0 16.0 1.0 N A:ASP66 5.0 15.5 1.0 O A:HOH2082 5.0 22.0 1.0

J.Ren, M.Kotaka, M.Lockyer, H.K.Lamb, A.R.Hawkins, D.K.Stammers. Gtp Cyclohydrolase II Structure and Mechanism. J.Biol.Chem. V. 280 36912 2005.
ISSN: ISSN 0021-9258
PubMed: 16115872
DOI: 10.1074/JBC.M507725200