Zinc in PDB 1b66: 6-Pyruvoyl Tetrahydropterin Synthase

All present enzymatic activity of 6-Pyruvoyl Tetrahydropterin Synthase:
4.6.1.10;

The structure of 6-Pyruvoyl Tetrahydropterin Synthase, PDB code: 1b66 was solved by T.Ploom, B.Thoeny, J.Yim, S.Lee, H.Nar, W.Leimbacher, R.Huber, J.Richardson, G.Auerbach, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.270, 120.270, 61.250, 90.00, 90.00, 120.00
R / Rfree (%)	22.7 / 25.8

The binding sites of Zinc atom in the 6-Pyruvoyl Tetrahydropterin Synthase (pdb code 1b66). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the 6-Pyruvoyl Tetrahydropterin Synthase, PDB code: 1b66:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the 6-Pyruvoyl Tetrahydropterin Synthase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 6-Pyruvoyl Tetrahydropterin Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:19.7 occ:1.00 NE2 A:HIS50 2.2 9.5 1.0 NE2 A:HIS23 2.2 13.6 1.0 NE2 A:HIS48 2.3 17.9 1.0 O9 A:BIO700 2.4 49.4 1.0 O10 A:BIO700 2.5 51.0 1.0 CD2 A:HIS48 3.0 18.2 1.0 CD2 A:HIS50 3.1 10.2 1.0 CE1 A:HIS23 3.2 15.1 1.0 C9 A:BIO700 3.2 50.3 1.0 CD2 A:HIS23 3.3 14.0 1.0 CE1 A:HIS50 3.3 8.0 1.0 C10 A:BIO700 3.3 51.6 1.0 CE1 A:HIS48 3.4 17.8 1.0 OE2 A:GLU133 3.5 18.5 1.0 C11 A:BIO700 3.9 52.4 1.0 CD A:GLU133 3.9 16.9 1.0 CG A:HIS48 4.3 18.1 1.0 CG A:HIS50 4.3 10.0 1.0 ND1 A:HIS23 4.3 15.2 1.0 ND1 A:HIS50 4.3 11.9 1.0 OE1 A:GLU133 4.4 18.0 1.0 ND1 A:HIS48 4.4 17.9 1.0 CG A:HIS23 4.4 15.1 1.0 C6 A:BIO700 4.6 48.7 1.0 CG A:GLU133 4.6 17.8 1.0 CB A:CYS42 4.8 13.2 1.0 O A:HOH717 4.8 19.4 1.0 N5 A:BIO700 4.9 47.2 1.0 OH A:TYR52 4.9 11.4 1.0

Zinc binding site 2 out of 2 in the 6-Pyruvoyl Tetrahydropterin Synthase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of 6-Pyruvoyl Tetrahydropterin Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:20.0 occ:1.00 NE2 B:HIS50 2.2 10.2 1.0 NE2 B:HIS48 2.2 18.2 1.0 NE2 B:HIS23 2.3 13.9 1.0 O9 B:BIO701 2.9 53.0 1.0 CD2 B:HIS48 2.9 17.6 1.0 CE1 B:HIS50 3.0 10.0 1.0 CE1 B:HIS23 3.1 14.3 1.0 CD2 B:HIS50 3.2 11.1 1.0 CD2 B:HIS23 3.3 16.0 1.0 CE1 B:HIS48 3.4 20.2 1.0 OE2 B:GLU133 3.5 20.7 1.0 O10 B:BIO701 3.9 55.6 1.0 CD B:GLU133 3.9 20.4 1.0 C9 B:BIO701 4.1 51.6 1.0 CG B:HIS48 4.2 18.4 1.0 ND1 B:HIS50 4.2 11.0 1.0 OE1 B:GLU133 4.3 21.6 1.0 ND1 B:HIS23 4.3 17.8 1.0 CG B:HIS50 4.3 10.4 1.0 ND1 B:HIS48 4.4 18.8 1.0 CG B:HIS23 4.4 16.7 1.0 C10 B:BIO701 4.5 54.1 1.0 CG B:GLU133 4.7 18.0 1.0 CB B:CYS42 4.7 20.5 1.0 C11 B:BIO701 4.8 56.0 1.0 OH B:TYR52 4.9 9.1 1.0 O B:HOH735 4.9 15.3 1.0

T.Ploom, B.Thony, J.Yim, S.Lee, H.Nar, W.Leimbacher, J.Richardson, R.Huber, G.Auerbach. Crystallographic and Kinetic Investigations on the Mechanism of 6-Pyruvoyl Tetrahydropterin Synthase. J.Mol.Biol. V. 286 851 1999.
ISSN: ISSN 0022-2836
PubMed: 10024455
DOI: 10.1006/JMBI.1998.2511