Zinc in PDB 4lao: Crystal Structure of Cordyceps Militaris Idcase H195A Mutant (Zn)

The structure of Crystal Structure of Cordyceps Militaris Idcase H195A Mutant (Zn), PDB code: 4lao was solved by S.Xu, W.Li, J.Zhu, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.33 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	144.365, 57.510, 105.563, 90.00, 105.31, 90.00
R / Rfree (%)	16.9 / 20.5

The binding sites of Zinc atom in the Crystal Structure of Cordyceps Militaris Idcase H195A Mutant (Zn) (pdb code 4lao). 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 Cordyceps Militaris Idcase H195A Mutant (Zn), PDB code: 4lao:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cordyceps Militaris Idcase H195A Mutant (Zn)


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 Cordyceps Militaris Idcase H195A Mutant (Zn) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:30.6 occ:1.00 NE2 A:HIS12 2.0 21.7 1.0 OD1 A:ASP323 2.1 20.4 1.0 NE2 A:HIS14 2.1 20.7 1.0 O A:HOH719 2.2 30.7 1.0 CG A:ASP323 2.9 21.9 1.0 CD2 A:HIS12 2.9 21.7 1.0 CD2 A:HIS14 3.0 21.3 1.0 CE1 A:HIS12 3.1 22.0 1.0 OD2 A:ASP323 3.1 23.4 1.0 CE1 A:HIS14 3.2 22.3 1.0 CG A:HIS12 4.1 21.1 1.0 ND1 A:HIS12 4.1 21.8 1.0 CB A:ASP323 4.2 19.9 1.0 CG A:HIS14 4.2 22.4 1.0 ND1 A:HIS14 4.3 23.2 1.0 NE2 A:HIS251 4.4 17.3 1.0 O A:HOH649 4.4 43.2 1.0 CD2 A:PHE326 4.5 30.0 1.0 CA A:ASP323 4.5 19.0 1.0 CE2 A:PHE326 4.6 32.8 1.0 O B:HOH529 4.8 29.7 1.0 CE1 A:HIS251 4.9 16.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cordyceps Militaris Idcase H195A Mutant (Zn)


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 Cordyceps Militaris Idcase H195A Mutant (Zn) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:34.3 occ:1.00 NE2 B:HIS12 2.1 25.8 1.0 OD1 B:ASP323 2.1 23.1 1.0 NE2 B:HIS14 2.1 28.4 1.0 O B:HOH658 2.2 32.1 1.0 CD2 B:HIS12 2.9 25.4 1.0 CG B:ASP323 2.9 24.3 1.0 CD2 B:HIS14 3.0 27.4 1.0 CE1 B:HIS14 3.1 30.0 1.0 CE1 B:HIS12 3.1 25.4 1.0 OD2 B:ASP323 3.2 26.2 1.0 CG B:HIS12 4.1 24.8 1.0 ND1 B:HIS12 4.2 25.7 1.0 CB B:ASP323 4.2 23.4 1.0 CG B:HIS14 4.2 28.5 1.0 ND1 B:HIS14 4.2 30.5 1.0 NE2 B:HIS251 4.4 21.8 1.0 CA B:ASP323 4.5 23.0 1.0 CD2 B:PHE326 4.5 38.7 1.0 CE2 B:PHE326 4.6 38.5 1.0 CE1 B:HIS251 4.9 23.0 1.0 O A:HOH631 5.0 44.7 1.0

S.Xu, W.Li, J.Zhu, R.Wang, Z.Li, G.L.Xu, J.Ding. Crystal Structures of Isoorotate Decarboxylases Reveal A Novel Catalytic Mechanism of 5-Carboxyl-Uracil Decarboxylation and Shed Light on the Search For Dna Decarboxylase. Cell Res. V. 23 1296 2013.
ISSN: ISSN 1001-0602
PubMed: 23917530
DOI: 10.1038/CR.2013.107