Zinc in PDB 5ch8: Crystal Structure of Mdla N225Q Mutant Form Penicillium Cyclopium

The structure of Crystal Structure of Mdla N225Q Mutant Form Penicillium Cyclopium, PDB code: 5ch8 was solved by J.Xu, H.Xu, S.Hou, J.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.32 / 1.62
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	33.330, 44.520, 44.760, 61.27, 68.65, 78.17
R / Rfree (%)	13.5 / 16.6

The structure of Crystal Structure of Mdla N225Q Mutant Form Penicillium Cyclopium also contains other interesting chemical elements:

Chlorine

(Cl)

5 atoms

The binding sites of Zinc atom in the Crystal Structure of Mdla N225Q Mutant Form Penicillium Cyclopium (pdb code 5ch8). 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 Mdla N225Q Mutant Form Penicillium Cyclopium, PDB code: 5ch8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Mdla N225Q Mutant Form Penicillium Cyclopium


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 Mdla N225Q Mutant Form Penicillium Cyclopium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:8.2 occ:1.00 OD2 A:ASP239 1.9 10.0 1.0 OD2 A:ASP237 2.0 6.8 1.0 O A:HOH606 2.1 9.6 1.0 CG A:ASP237 2.7 6.7 1.0 OD1 A:ASP237 2.7 6.6 1.0 CG A:ASP239 2.9 9.8 1.0 CB A:ASP239 3.4 8.4 1.0 OD1 A:ASP239 4.0 12.0 1.0 CB A:ASP237 4.1 6.3 1.0 CA A:ASP239 4.7 8.1 1.0 O A:HOH547 4.7 6.6 1.0 O A:HOH611 4.8 25.5 1.0 N A:ASP239 4.8 7.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Mdla N225Q Mutant Form Penicillium Cyclopium


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 Mdla N225Q Mutant Form Penicillium Cyclopium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:15.3 occ:0.40 OE2 A:GLU43 2.0 14.8 1.0 OD1 A:ASP8 2.0 9.9 0.5 O A:HOH408 2.1 18.2 1.0 CD A:GLU43 2.9 11.7 1.0 CG A:ASP8 2.9 9.3 0.5 OE1 A:GLU43 3.1 14.0 1.0 OD2 A:ASP8 3.2 9.8 0.5 CB A:ASP8 4.3 9.1 0.5 CB A:ASP8 4.3 10.2 0.6 O A:ASP8 4.3 9.0 1.0 CG A:GLU43 4.3 9.6 1.0 CG A:ASP8 4.4 11.1 0.6 CA A:ASP8 4.6 9.1 0.6 CA A:ASP8 4.6 8.7 0.5 OD1 A:ASP8 4.7 12.8 0.6 C A:ASP8 4.8 8.8 1.0 OD2 A:ASP8 4.9 12.8 0.6

Q.Tang, G.M.Popowicz, X.Wang, J.Liu, I.V.Pavlidis, Y.Wang. Lipase-Driven Epoxidation Is A Two-Stage Synergistic Process Chemistryselect V. 4 836 2016.
ISSN: ESSN 2365-6549
DOI: 10.1002/SLCT.201600254