Zinc in PDB 6z89: 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: 6z89 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)	105.47 / 2.37
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.786, 121.786, 357.150, 90.00, 90.00, 120.00
R / Rfree (%)	23.4 / 23.8

The binding sites of Zinc atom in the Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor (pdb code 6z89). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor, PDB code: 6z89:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 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 A:Zn302 b:0.4 occ:1.00 NE2 A:HIS144 2.7 81.4 1.0 CB A:HIS210 3.5 77.0 1.0 ND1 A:HIS210 3.5 83.3 1.0 SG A:CYS141 3.6 78.0 1.0 CE1 A:HIS144 3.6 82.1 1.0 CD2 A:HIS144 3.8 79.5 1.0 CG A:HIS210 3.8 80.6 1.0 CB A:CYS141 4.1 65.5 1.0 CE1 A:HIS210 4.6 83.5 1.0 CA A:HIS210 4.6 75.5 1.0 C A:HIS210 4.9 76.2 1.0 ND1 A:HIS144 4.9 80.4 1.0 CG A:HIS144 4.9 77.0 1.0 CD2 A:HIS210 4.9 82.1 1.0 O A:HIS210 5.0 77.0 1.0

Zinc binding site 2 out of 5 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 B:Zn301 b:0.2 occ:1.00 SG B:CYS212 2.6 96.1 1.0 SG B:CYS141 2.8 72.8 1.0 O B:HOH419 2.9 57.9 1.0 CB B:CYS212 3.0 91.2 1.0 ND1 B:HIS144 3.4 59.1 1.0 CE1 B:HIS144 3.8 59.7 1.0 CB B:CYS141 3.9 60.5 1.0 ND1 B:HIS210 4.2 74.6 1.0 O B:HOH408 4.4 54.1 1.0 CA B:CYS212 4.5 89.5 1.0 CD1 C:LEU165 4.6 92.6 1.0 CB C:LEU165 4.6 90.9 1.0 ND1 B:HIS143 4.7 63.5 1.0 CB B:HIS143 4.7 57.4 1.0 CG B:HIS144 4.7 57.1 1.0 CG C:LEU165 4.8 92.2 1.0 O B:HOH420 4.9 62.7 1.0 CB B:HIS210 4.9 72.3 1.0 CG B:HIS210 5.0 72.8 1.0 N B:CYS212 5.0 86.4 1.0

Zinc binding site 3 out of 5 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 3 of Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:0.1 occ:1.00 ND1 C:HIS144 2.0 0.9 1.0 SG C:CYS212 2.5 0.1 1.0 SG C:CYS141 2.7 0.8 1.0 CE1 C:HIS144 2.8 0.5 1.0 CG C:HIS144 3.2 0.9 1.0 CB C:CYS212 3.6 0.6 1.0 CB C:HIS144 3.8 0.0 1.0 CB C:CYS141 3.9 0.5 1.0 N C:HIS144 4.0 0.2 1.0 NE2 C:HIS144 4.0 0.3 1.0 CB C:HIS143 4.2 0.1 1.0 CD2 C:HIS144 4.3 0.1 1.0 CG2 C:VAL146 4.4 0.8 1.0 CA C:HIS144 4.5 0.8 1.0 C C:HIS143 4.8 0.9 1.0 CA C:HIS143 4.9 0.3 1.0 CA C:CYS212 5.0 0.6 1.0

Zinc binding site 4 out of 5 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 4 of Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:0.5 occ:1.00 NE2 D:HIS144 2.7 81.8 1.0 O D:HOH407 3.3 76.7 1.0 CB D:HIS210 3.3 84.1 1.0 CE1 D:HIS144 3.4 82.7 1.0 ND1 D:HIS210 3.6 90.6 1.0 CG D:HIS210 3.9 87.9 1.0 CD2 D:HIS144 3.9 79.9 1.0 SG D:CYS141 3.9 79.2 1.0 CA D:HIS210 4.5 83.1 1.0 CB D:CYS141 4.5 69.0 1.0 C D:HIS210 4.6 83.8 1.0 CD1 E:LEU165 4.6 0.2 1.0 ND1 D:HIS144 4.7 81.8 1.0 CE1 D:HIS210 4.8 91.1 1.0 O D:HIS210 4.9 84.2 1.0 CG D:HIS144 4.9 78.2 1.0

Zinc binding site 5 out of 5 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 5 of Human Gtp Cyclohydrolase I in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn301 b:93.3 occ:1.00 ND1 E:HIS144 2.2 52.8 1.0 SG E:CYS141 2.3 63.4 1.0 SG E:CYS212 2.5 92.8 1.0 CB E:CYS212 2.6 84.8 1.0 CE1 E:HIS144 3.0 52.5 1.0 CG E:HIS144 3.4 51.9 1.0 CB E:CYS141 3.6 57.1 1.0 CB E:HIS144 3.9 52.0 1.0 CB E:HIS143 4.0 54.5 1.0 N E:HIS144 4.0 53.8 1.0 O E:HOH411 4.0 69.7 1.0 CA E:CYS212 4.1 83.0 1.0 NE2 E:HIS144 4.2 52.4 1.0 O E:HOH409 4.4 57.8 1.0 CD2 E:HIS144 4.4 52.3 1.0 CA E:HIS144 4.6 54.0 1.0 C E:HIS143 4.7 54.0 1.0 ND1 E:HIS143 4.7 59.7 1.0 O E:CYS212 4.7 85.6 1.0 CA E:HIS143 4.7 54.0 1.0 C E:CYS212 4.7 84.7 1.0 N E:HIS143 4.8 54.2 1.0 CG E:HIS143 4.8 57.7 1.0 N E:CYS212 4.9 80.5 1.0 CA E:CYS141 4.9 56.6 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