Zinc in PDB 4j5h: Crystal Structure of B. Thuringiensis Aiia Mutant F107W with N- Decanoyl-L-Homoserine Bound at the Active Site

All present enzymatic activity of Crystal Structure of B. Thuringiensis Aiia Mutant F107W with N- Decanoyl-L-Homoserine Bound at the Active Site:
3.1.1.81;

The structure of Crystal Structure of B. Thuringiensis Aiia Mutant F107W with N- Decanoyl-L-Homoserine Bound at the Active Site, PDB code: 4j5h 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)	32.57 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.825, 55.444, 80.396, 90.00, 90.00, 90.00
R / Rfree (%)	12 / 15.1

The binding sites of Zinc atom in the Crystal Structure of B. Thuringiensis Aiia Mutant F107W with N- Decanoyl-L-Homoserine Bound at the Active Site (pdb code 4j5h). 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 with N- Decanoyl-L-Homoserine Bound at the Active Site, PDB code: 4j5h:
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 with N- Decanoyl-L-Homoserine Bound at the Active Site


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 with N- Decanoyl-L-Homoserine Bound at the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:16.2 occ:1.00 OXT A:1K4303 1.8 23.6 1.0 OD2 A:ASP191 2.0 12.8 1.0 NE2 A:HIS109 2.0 12.7 1.0 NE2 A:HIS235 2.0 15.3 1.0 OD1 A:ASP191 2.6 15.4 1.0 CG A:ASP191 2.6 13.8 1.0 C A:1K4303 2.9 18.8 1.0 CE1 A:HIS109 3.0 12.6 1.0 CD2 A:HIS235 3.0 15.6 1.0 CD2 A:HIS109 3.0 11.6 1.0 CE1 A:HIS235 3.0 16.4 1.0 O A:1K4303 3.3 22.4 1.0 OD2 A:ASP108 3.6 29.9 1.0 ZN A:ZN302 3.7 13.7 1.0 OD1 A:ASP108 4.0 16.9 1.0 CB A:ASP191 4.1 12.6 1.0 ND1 A:HIS109 4.1 11.1 1.0 ND1 A:HIS235 4.1 18.5 1.0 CG A:HIS109 4.1 10.3 1.0 CG A:HIS235 4.2 15.1 1.0 CG A:ASP108 4.2 16.9 1.0 CA A:1K4303 4.2 16.6 1.0 CE1 A:HIS104 4.2 11.8 1.0 CE1 A:TYR194 4.2 18.5 1.0 CB A:1K4303 4.4 19.8 1.0 NE2 A:HIS104 4.4 13.6 1.0 O A:HOH478 4.6 35.8 1.0 CD1 A:TYR194 4.9 17.5 1.0 CZ A:TYR194 4.9 16.8 1.0 OH A:TYR194 5.0 20.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of B. Thuringiensis Aiia Mutant F107W with N- Decanoyl-L-Homoserine Bound at the Active Site


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 with N- Decanoyl-L-Homoserine Bound at the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:13.7 occ:1.00 O A:1K4303 1.9 22.4 1.0 NE2 A:HIS169 2.1 13.7 1.0 NE2 A:HIS104 2.1 13.6 1.0 ND1 A:HIS106 2.2 12.2 1.0 OD2 A:ASP191 2.4 12.8 1.0 CD2 A:HIS104 3.0 12.0 1.0 CD2 A:HIS169 3.0 13.4 1.0 C A:1K4303 3.0 18.8 1.0 CE1 A:HIS169 3.1 14.0 1.0 CE1 A:HIS106 3.1 13.6 1.0 CE1 A:HIS104 3.1 11.8 1.0 CG A:HIS106 3.2 11.6 1.0 CG A:ASP191 3.5 13.8 1.0 OXT A:1K4303 3.5 23.6 1.0 CB A:HIS106 3.6 11.3 1.0 ZN A:ZN301 3.7 16.2 1.0 CB A:ASP191 3.8 12.6 1.0 CG A:HIS169 4.2 13.6 1.0 ND1 A:HIS169 4.2 14.5 1.0 CG A:HIS104 4.2 10.9 1.0 ND1 A:HIS104 4.2 10.7 1.0 NE2 A:HIS106 4.2 14.5 1.0 CD2 A:HIS109 4.2 11.6 1.0 CA A:1K4303 4.3 16.6 1.0 CD2 A:HIS106 4.3 13.7 1.0 NE2 A:HIS109 4.3 12.7 1.0 N A:1K4303 4.4 20.2 1.0 OH A:TYR194 4.4 20.2 1.0 CAQ A:1K4303 4.5 19.3 1.0 OAB A:1K4303 4.5 19.8 1.0 OD1 A:ASP191 4.6 15.4 1.0 CE1 A:TYR194 4.7 18.5 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