Zinc in PDB 6z88: Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor

All present enzymatic activity of Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor:
3.5.4.16;

The structure of Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor, PDB code: 6z88 was solved by R.Ebenhoch, H.Nar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	135.82 / 2.69
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	112.355, 161.505, 271.642, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 25.4

The binding sites of Zinc atom in the Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor (pdb code 6z88). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor, PDB code: 6z88:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:0.7 occ:1.00 ND1 B:HIS144 2.1 81.0 1.0 CG B:HIS144 2.8 77.6 1.0 CB B:HIS144 2.8 71.5 1.0 CB B:CYS141 3.0 71.0 1.0 SG B:CYS141 3.0 78.8 1.0 N B:HIS144 3.2 68.3 1.0 CE1 B:HIS144 3.3 82.1 1.0 CA B:HIS144 3.4 68.5 1.0 CB B:VAL146 3.8 58.6 1.0 C B:HIS144 3.9 66.5 1.0 N B:VAL146 3.9 59.9 1.0 CG2 B:VAL146 4.0 58.5 1.0 N B:LEU145 4.1 64.0 1.0 CD2 B:HIS144 4.1 79.4 1.0 O B:VAL146 4.2 57.9 1.0 O B:CYS141 4.2 69.7 1.0 CA B:CYS141 4.3 68.9 1.0 NE2 B:HIS144 4.3 81.2 1.0 C B:HIS143 4.3 68.9 1.0 CA B:VAL146 4.4 58.6 1.0 C B:CYS141 4.5 69.1 1.0 O B:HIS144 4.6 67.5 1.0 CB B:HIS143 4.6 69.7 1.0 N B:HIS143 4.7 67.9 1.0 CA B:HIS143 4.7 68.5 1.0 C B:VAL146 4.8 57.3 1.0 C B:LEU145 4.9 61.5 1.0 N B:CYS141 5.0 67.8 1.0

Zinc binding site 2 out of 2 in the Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn301 b:1.0 occ:1.00 O F:HIS210 4.1 77.8 1.0 C F:HIS210 4.3 77.6 1.0 CB F:HIS210 4.3 78.5 1.0 CE1 F:HIS144 4.6 78.6 1.0 ND1 F:HIS144 4.7 77.8 1.0 CA F:HIS210 5.0 77.0 1.0

R.Ebenhoch, S.Prinz, S.Kaltwasser, D.J.Mills, R.Meinecke, M.Rubbelke, D.Reinert, M.Bauer, L.Weixler, M.Zeeb, J.Vonck, H.Nar. A Hybrid Approach Reveals the Allosteric Regulation of Gtp Cyclohydrolase I. Proc.Natl.Acad.Sci.Usa 2020.
ISSN: ESSN 1091-6490
PubMed: 33229582
DOI: 10.1073/PNAS.2013473117