Zinc in PDB 4g1p: Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae

The structure of Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae, PDB code: 4g1p was solved by A.K.Singh, M.Singh, V.K.Pandya, V.Singh, M.Mittal, S.Kumaran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.73 / 2.55
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	119.132, 119.132, 176.302, 90.00, 90.00, 120.00
R / Rfree (%)	18.6 / 23.1

The binding sites of Zinc atom in the Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae (pdb code 4g1p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae, PDB code: 4g1p:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:21.9 occ:1.00 OD2 A:ASP137 2.0 17.3 1.0 NE2 A:HIS450 2.0 21.8 1.0 OE2 A:GLU172 2.1 18.0 1.0 CA A:GLY503 2.4 20.2 1.0 N A:GLY503 2.6 20.0 1.0 OE1 A:GLU172 2.6 20.5 1.0 CD A:GLU172 2.7 19.9 1.0 CG A:ASP137 2.9 17.0 1.0 CD2 A:HIS450 3.0 21.0 1.0 OD1 A:ASP137 3.0 18.5 1.0 CE1 A:HIS450 3.0 21.8 1.0 C A:GLY503 3.6 30.3 1.0 N A:CYS504 3.8 36.0 1.0 O A:HOH601 3.9 13.7 1.0 ZN A:ZN502 4.0 76.9 1.0 OE1 A:GLU171 4.0 25.3 1.0 ND1 A:HIS450 4.1 21.6 1.0 CG A:HIS450 4.1 19.5 1.0 CG A:GLU172 4.2 16.9 1.0 CB A:ASP137 4.3 15.7 1.0 CG A:GLN106 4.5 18.2 1.0 CE1 A:HIS102 4.5 17.7 1.0 NE2 A:HIS102 4.6 18.2 1.0 O A:GLY503 4.7 32.6 1.0 NE2 A:GLN106 4.7 21.9 1.0 O A:HOH602 4.9 17.3 1.0 O A:ASP137 5.0 16.0 1.0

Zinc binding site 2 out of 2 in the Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural and Mechanistic Basis of Substrate Recognition By Novel Di- Peptidase DUG1P From Saccharomyces Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:76.9 occ:1.00 OD1 A:ASP200 2.7 23.1 1.0 OD1 A:ASP137 2.9 18.5 1.0 O A:ASP200 3.2 22.0 1.0 CA A:GLY503 3.3 20.2 1.0 O A:HOH605 3.3 25.0 1.0 N A:GLY503 3.3 20.0 1.0 CG A:ASP200 3.4 23.7 1.0 CG A:ASP137 3.5 17.0 1.0 O A:HOH768 3.6 35.5 1.0 OD2 A:ASP137 3.8 17.3 1.0 OH A:TYR202 3.8 29.0 1.0 NE2 A:HIS102 3.8 18.2 1.0 OD2 A:ASP200 3.8 27.1 1.0 ZN A:ZN501 4.0 21.9 1.0 C A:ASP200 4.1 20.5 1.0 OE2 A:GLU171 4.1 28.2 1.0 CB A:ASP200 4.3 21.6 1.0 CB A:ASP137 4.5 15.7 1.0 C A:GLY503 4.5 30.3 1.0 CA A:ASP200 4.5 19.6 1.0 OE1 A:GLU171 4.6 25.3 1.0 CD2 A:HIS102 4.6 20.3 1.0 CD A:GLU171 4.6 29.1 1.0 CZ A:TYR202 4.7 26.0 1.0 O A:GLY503 4.8 32.6 1.0 CE1 A:HIS102 4.8 17.7 1.0 CA A:ASP137 5.0 16.9 1.0

A.K.Singh, M.Singh, V.K.Pandya, V.Singh, M.Mittal, S.Kumaran. Structural and Mechanistic Basis of Substrate Recognition By Novel Di-Peptidase DUG1P From Saccromyces Cerevesiae To Be Published.