Zinc in PDB 5br4: E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant

All present enzymatic activity of E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant:
1.1.1.77;

The structure of E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant, PDB code: 5br4 was solved by J.K.B.Cahn, S.Brinkmann-Chen, F.H.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	85.50 / 0.91
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.697, 63.769, 91.674, 90.00, 111.15, 90.00
R / Rfree (%)	12.9 / 14.7

The structure of E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Zinc atom in the E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant (pdb code 5br4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant, PDB code: 5br4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:7.6 occ:1.00 OD1 A:ASP196 2.0 7.8 1.0 NE2 A:HIS277 2.0 7.6 1.0 NE2 A:HIS263 2.1 7.3 1.0 NE2 A:HIS200 2.1 8.0 1.0 OD2 A:ASP196 2.7 7.7 1.0 CG A:ASP196 2.7 7.5 1.0 CE1 A:HIS263 2.9 7.7 1.0 CE1 A:HIS277 2.9 8.2 1.0 CD2 A:HIS200 3.0 7.3 1.0 CE1 A:HIS200 3.0 7.8 1.0 CD2 A:HIS277 3.0 7.5 1.0 CD2 A:HIS263 3.1 7.7 1.0 ND2 A:ASN281 3.8 7.9 1.0 C5N A:NAD402 4.0 8.2 1.0 ND1 A:HIS277 4.1 8.1 1.0 ND1 A:HIS200 4.1 8.0 1.0 CB A:ASP196 4.1 8.4 1.0 CG A:ASN281 4.1 7.4 1.0 CG A:HIS200 4.1 7.3 1.0 CG A:HIS277 4.1 7.5 1.0 ND1 A:HIS263 4.1 7.3 1.0 CG A:HIS263 4.2 7.3 1.0 O A:ASP196 4.3 7.4 1.0 C6N A:NAD402 4.3 7.9 1.0 OD1 A:ASN281 4.5 8.5 1.0 CB A:ASN281 4.6 7.5 1.0 CA A:ASP196 4.7 8.1 1.0 C A:ASP196 4.7 7.3 1.0

Zinc binding site 2 out of 2 in the E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E. Coli Lactaldehyde Reductase (Fuco) M185C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:8.5 occ:1.00 NE2 B:HIS277 2.0 8.0 1.0 OD1 B:ASP196 2.0 8.6 1.0 NE2 B:HIS263 2.0 8.7 1.0 NE2 B:HIS200 2.1 9.2 1.0 CG B:ASP196 2.7 9.0 1.0 OD2 B:ASP196 2.7 8.5 1.0 CE1 B:HIS263 2.9 8.7 1.0 CE1 B:HIS277 3.0 9.5 1.0 CD2 B:HIS200 3.0 7.8 1.0 CE1 B:HIS200 3.0 8.9 1.0 CD2 B:HIS277 3.0 8.1 1.0 CD2 B:HIS263 3.1 7.9 1.0 ND2 B:ASN281 3.8 8.8 1.0 C5N B:NAD402 4.0 9.6 1.0 ND1 B:HIS277 4.1 9.8 1.0 CB B:ASP196 4.1 9.1 1.0 ND1 B:HIS200 4.1 8.3 1.0 CG B:HIS277 4.1 8.9 1.0 CG B:ASN281 4.1 8.6 1.0 CG B:HIS200 4.1 7.6 1.0 ND1 B:HIS263 4.1 8.5 1.0 CG B:HIS263 4.2 8.2 1.0 O B:ASP196 4.3 7.2 1.0 C6N B:NAD402 4.4 9.6 1.0 OD1 B:ASN281 4.5 9.5 1.0 CA B:ASP196 4.7 8.1 1.0 CB B:ASN281 4.7 8.5 1.0 C B:ASP196 4.7 7.3 1.0

J.K.Cahn, A.Baumschlager, S.Brinkmann-Chen, F.H.Arnold. Mutations in Adenine-Binding Pockets Enhance Catalytic Properties of Nad(P)H-Dependent Enzymes. Protein Eng.Des.Sel. V. 29 31 2016.
ISSN: ESSN 1741-0134
PubMed: 26512129
DOI: 10.1093/PROTEIN/GZV057