Nickel in PDB 4g9g: Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant

The structure of Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant, PDB code: 4g9g was solved by D.C.Liang, X.X.Yan, A.Gao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.87 / 1.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.378, 129.567, 44.728, 90.00, 111.02, 90.00
R / Rfree (%)	14.1 / 17.7

The binding sites of Nickel atom in the Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant (pdb code 4g9g). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant, PDB code: 4g9g:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni301 b:10.4 occ:0.44 SG A:CYS165 2.3 16.8 1.0 O A:HOH970 2.6 46.7 0.7 O A:HOH969 2.8 26.0 0.8 CB A:CYS165 3.6 18.1 1.0 CG2 A:VAL177 3.7 13.5 1.0 OG1 A:THR164 3.8 18.1 1.0 CA A:ALA161 3.9 19.3 1.0 O A:ALA161 4.1 13.5 1.0 CB A:ALA161 4.1 19.0 1.0 CB A:LEU173 4.2 13.7 1.0 CD2 A:LEU173 4.3 16.1 1.0 C A:ALA161 4.5 15.8 1.0 O A:LEU173 4.5 16.8 1.0 N A:CYS165 4.6 12.6 1.0 CD1 A:LEU173 4.6 17.0 1.0 CG A:LEU173 4.6 14.6 1.0 CA A:CYS165 4.6 13.5 1.0 CD1 A:ILE39 4.7 15.8 1.0 CB A:SER35 4.8 8.4 0.5 OG A:SER35 4.8 11.3 0.5 CA A:LEU173 4.8 15.9 1.0 N A:ALA161 5.0 16.3 1.0

Nickel binding site 2 out of 2 in the Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Crystal Structures of N-Acyl Homoserine Lactonase Aidh E219G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni301 b:11.5 occ:0.50 SG B:CYS165 2.3 16.9 1.0 O B:HOH851 2.6 50.9 0.7 O B:HOH852 2.8 44.6 0.7 O B:HOH601 2.8 34.5 0.9 CB B:CYS165 3.6 13.9 1.0 CG2 B:VAL177 3.7 10.4 1.0 OG1 B:THR164 3.8 6.4 0.5 CA B:ALA161 3.9 13.3 1.0 O B:ALA161 4.0 12.2 1.0 CB B:ALA161 4.0 14.2 1.0 CB B:LEU173 4.2 14.4 1.0 O B:LEU173 4.3 12.8 1.0 C B:ALA161 4.4 11.5 1.0 CD2 B:LEU173 4.4 21.2 1.0 N B:CYS165 4.5 11.7 1.0 CA B:CYS165 4.6 11.6 1.0 CG B:LEU173 4.7 15.2 1.0 CA B:LEU173 4.8 13.0 1.0 CB B:SER35 4.8 10.8 0.4 C B:LEU173 4.8 12.9 1.0 CD1 B:LEU173 4.8 15.6 1.0 CB B:THR164 4.9 9.3 0.5 CD1 B:ILE39 4.9 12.8 1.0 OG B:SER35 4.9 9.4 0.6

A.Gao, G.Y.Mei, S.Liu, P.Wang, Q.Tang, Y.P.Liu, H.Wen, X.M.An, L.Q.Zhang, X.X.Yan, D.C.Liang. High-Resolution Structures of Aidh Complexes Provide Insights Into A Novel Catalytic Mechanism For N-Acyl Homoserine Lactonase Acta Crystallogr.,Sect.D V. 69 82 2013.
ISSN: ISSN 0907-4449
PubMed: 23275166
DOI: 10.1107/S0907444912042369