Zinc in PDB 2bz0: Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc

All present enzymatic activity of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc:
3.5.4.25;

The structure of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc, PDB code: 2bz0 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)	24.03 / 2.6
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.080, 99.080, 96.290, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 26

The structure of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc (pdb code 2bz0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc, PDB code: 2bz0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc


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 Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1174 b:75.1 occ:1.00 SG A:CYS54 2.2 40.5 1.0 SG A:CYS67 2.3 63.0 1.0 SG A:CYS65 2.5 57.5 1.0 O A:HOH2044 3.1 57.0 1.0 CB A:CYS65 3.3 62.6 1.0 CB A:CYS54 3.3 36.5 1.0 CB A:CYS67 3.4 55.3 1.0 C8 A:G2P1176 3.8 0.7 1.0 C2' A:G2P1176 3.9 93.8 1.0 O2' A:G2P1176 4.1 81.2 1.0 O A:HOH2031 4.2 46.0 1.0 OH A:TYR105 4.3 82.0 1.0 N7 A:G2P1176 4.4 1.0 1.0 N9 A:G2P1176 4.5 1.0 1.0 OG1 A:THR56 4.5 57.8 1.0 NZ A:LYS101 4.5 0.4 1.0 N A:CYS67 4.5 51.5 1.0 CA A:CYS67 4.6 53.4 1.0 CA A:CYS54 4.7 34.8 1.0 CA A:CYS65 4.7 66.0 1.0 C1' A:G2P1176 4.8 99.1 1.0 N A:GLY57 4.8 42.1 1.0 C3' A:G2P1176 4.9 83.7 1.0 CA A:GLY57 4.9 39.6 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1174 b:97.1 occ:1.00 SG B:CYS67 2.3 68.7 1.0 SG B:CYS54 2.4 49.3 1.0 SG B:CYS65 2.6 87.1 1.0 C8 B:G2P1175 3.0 0.4 1.0 CB B:CYS65 3.2 76.2 1.0 CB B:CYS54 3.5 35.9 1.0 CB B:CYS67 3.5 72.8 1.0 N7 B:G2P1175 3.6 0.3 1.0 O B:HOH2015 3.8 44.4 1.0 C2' B:G2P1175 3.9 0.8 1.0 N9 B:G2P1175 4.0 0.1 1.0 OH B:TYR105 4.1 72.2 1.0 O2' B:G2P1175 4.4 78.2 1.0 OG1 B:THR56 4.5 53.7 1.0 C1' B:G2P1175 4.5 0.1 1.0 NZ B:LYS101 4.5 72.2 1.0 N B:CYS67 4.6 75.8 1.0 CA B:CYS67 4.7 72.4 1.0 CA B:CYS65 4.7 73.3 1.0 CA B:CYS54 4.8 44.0 1.0 C5 B:G2P1175 4.8 1.0 1.0 N B:GLY57 4.9 34.5 1.0 C3' B:G2P1175 4.9 0.0 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