Zinc in PDB 4j5f: Crystal Structure of B. Thuringiensis Aiia Mutant F107W

All present enzymatic activity of Crystal Structure of B. Thuringiensis Aiia Mutant F107W:
3.1.1.81;

The structure of Crystal Structure of B. Thuringiensis Aiia Mutant F107W, PDB code: 4j5f was solved by C.F.Liu, D.Liu, J.Momb, P.W.Thomas, A.Lajoie, G.A.Petsko, W.Fast, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.23 / 1.72
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.602, 55.996, 81.250, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 20.9

The binding sites of Zinc atom in the Crystal Structure of B. Thuringiensis Aiia Mutant F107W (pdb code 4j5f). 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 B. Thuringiensis Aiia Mutant F107W, PDB code: 4j5f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of B. Thuringiensis Aiia Mutant F107W


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 B. Thuringiensis Aiia Mutant F107W within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:33.1 occ:1.00 NE2 A:HIS109 2.0 29.4 1.0 OD2 A:ASP191 2.0 32.1 1.0 NE2 A:HIS235 2.0 26.0 1.0 OD2 A:ASP108 2.4 34.8 1.0 O A:HOH401 2.5 54.6 1.0 CD2 A:HIS109 2.9 25.9 1.0 CD2 A:HIS235 2.9 32.3 1.0 CG A:ASP191 3.0 33.1 1.0 CE1 A:HIS109 3.0 32.1 1.0 CE1 A:HIS235 3.1 31.6 1.0 OD1 A:ASP191 3.3 31.5 1.0 CG A:ASP108 3.3 30.2 1.0 ZN A:ZN302 3.5 32.3 1.0 OD1 A:ASP108 3.6 30.4 1.0 O A:HOH428 4.0 37.1 1.0 CG A:HIS109 4.1 28.4 1.0 ND1 A:HIS109 4.1 32.0 1.0 CG A:HIS235 4.1 34.5 1.0 ND1 A:HIS235 4.2 33.5 1.0 NE2 A:HIS104 4.2 29.9 1.0 CE1 A:HIS104 4.3 25.8 1.0 CB A:ASP191 4.3 29.6 1.0 OH A:TYR194 4.6 42.6 1.0 O A:HOH470 4.6 37.8 1.0 CB A:ASP108 4.7 28.7 1.0 NE2 A:HIS169 4.7 29.6 1.0 CE1 A:TYR194 4.8 37.6 1.0 CZ A:TYR194 4.9 42.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of B. Thuringiensis Aiia Mutant F107W


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 B. Thuringiensis Aiia Mutant F107W within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:32.3 occ:1.00 NE2 A:HIS169 2.0 29.6 1.0 ND1 A:HIS106 2.1 30.0 1.0 NE2 A:HIS104 2.2 29.9 1.0 OD2 A:ASP191 2.7 32.1 1.0 O A:HOH401 2.8 54.6 1.0 CD2 A:HIS169 2.9 26.3 1.0 CE1 A:HIS106 2.9 31.9 1.0 CD2 A:HIS104 3.0 24.1 1.0 CE1 A:HIS169 3.1 30.6 1.0 CG A:HIS106 3.2 31.5 1.0 CE1 A:HIS104 3.2 25.8 1.0 ZN A:ZN301 3.5 33.1 1.0 CB A:HIS106 3.6 25.6 1.0 CG A:ASP191 3.7 33.1 1.0 CD2 A:HIS109 4.0 25.9 1.0 CB A:ASP191 4.0 29.6 1.0 NE2 A:HIS109 4.0 29.4 1.0 CG A:HIS169 4.1 30.1 1.0 NE2 A:HIS106 4.1 32.3 1.0 ND1 A:HIS169 4.1 28.9 1.0 CG A:HIS104 4.2 26.7 1.0 CD2 A:HIS106 4.2 30.0 1.0 ND1 A:HIS104 4.3 27.4 1.0 OD1 A:ASP108 4.4 30.4 1.0 OH A:TYR194 4.5 42.6 1.0 OD1 A:ASP191 4.9 31.5 1.0 OD2 A:ASP108 4.9 34.8 1.0 CE1 A:TYR194 5.0 37.6 1.0 CE1 A:HIS109 5.0 32.1 1.0

C.F.Liu, D.Liu, J.Momb, P.W.Thomas, A.Lajoie, G.A.Petsko, W.Fast, D.Ringe. A Phenylalanine Clamp Controls Substrate Specificity in the Quorum-Quenching Metallo-Gamma-Lactonase From Bacillus Thuringiensis. Biochemistry V. 52 1603 2013.
ISSN: ISSN 0006-2960
PubMed: 23387521
DOI: 10.1021/BI400050J