Zinc in PDB 5k9g: Crystal Structure of Gtp Cyclohydrolase-Ib with Tris

All present enzymatic activity of Crystal Structure of Gtp Cyclohydrolase-Ib with Tris:
3.5.4.16;

The structure of Crystal Structure of Gtp Cyclohydrolase-Ib with Tris, PDB code: 5k9g was solved by J.Alvarez, B.Stec, M.A.Swairjo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.16 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	92.707, 100.557, 114.017, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 22.1

The binding sites of Zinc atom in the Crystal Structure of Gtp Cyclohydrolase-Ib with Tris (pdb code 5k9g). 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 Gtp Cyclohydrolase-Ib with Tris, PDB code: 5k9g:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Gtp Cyclohydrolase-Ib with Tris


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 Gtp Cyclohydrolase-Ib with Tris within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:56.4 occ:1.00 NE2 A:HIS159 2.3 46.2 1.0 SG A:CYS147 2.4 51.6 1.0 O A:HOH474 2.7 64.7 1.0 CD2 A:HIS159 3.0 46.6 1.0 CB A:CYS147 3.3 51.5 1.0 CE1 A:HIS159 3.4 54.8 1.0 OE1 A:GLU243 4.0 85.6 1.0 CG A:HIS159 4.3 54.2 1.0 CD1 A:ILE245 4.3 56.6 1.0 ND1 A:HIS159 4.4 46.2 1.0 CB A:SER150 4.5 64.6 1.0 N A:SER150 4.5 60.3 1.0 CA A:CYS147 4.7 53.1 1.0 CB A:SNC149 4.8 60.1 1.0 CA A:SER150 5.0 56.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Gtp Cyclohydrolase-Ib with Tris


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 Gtp Cyclohydrolase-Ib with Tris within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:35.6 occ:1.00 N B:TRS302 2.0 42.1 1.0 NE2 B:HIS159 2.2 32.0 1.0 SG B:CYS147 2.4 35.5 1.0 O3 B:TRS302 2.5 36.9 1.0 C B:TRS302 3.0 46.4 1.0 CD2 B:HIS159 3.1 30.3 1.0 CB B:CYS147 3.2 32.9 1.0 CE1 B:HIS159 3.2 31.1 1.0 C3 B:TRS302 3.2 45.2 1.0 C1 B:TRS302 3.5 50.2 1.0 CG B:HIS159 4.3 29.9 1.0 ND1 B:HIS159 4.3 31.0 1.0 CB B:SER150 4.3 32.1 1.0 O1 B:FMT309 4.3 62.1 1.0 C2 B:TRS302 4.3 46.8 1.0 OE2 B:GLU243 4.4 43.7 1.0 CD1 B:ILE245 4.4 33.8 1.0 N B:SER150 4.4 37.5 1.0 O2 B:TRS302 4.5 50.4 1.0 O1 B:TRS302 4.6 61.9 1.0 CA B:CYS147 4.7 32.2 1.0 CA B:SER150 4.9 34.1 1.0 CB B:SNC149 4.9 35.4 1.0

N.Paranagama, S.A.Bonnett, J.Alvarez, A.Luthra, B.Stec, A.Gustafson, D.Iwata-Reuyl, M.A.Swairjo. Mechanism and Catalytic Strategy of the Prokaryotic-Specific Gtp Cyclohydrolase-Ib. Biochem.J. V. 474 1017 2017.
ISSN: ESSN 1470-8728
PubMed: 28126741
DOI: 10.1042/BCJ20161025