Zinc in PDB 2zj7: Crystal Structure of D157A Mutant of Pseudomonas Sp. MIS38 Lipase

All present enzymatic activity of Crystal Structure of D157A Mutant of Pseudomonas Sp. MIS38 Lipase:
3.1.1.3;

The structure of Crystal Structure of D157A Mutant of Pseudomonas Sp. MIS38 Lipase, PDB code: 2zj7 was solved by C.Angkawidjaja, K.Kuwahara, S.Kanaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.21
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.634, 84.627, 87.521, 90.00, 96.85, 90.00
R / Rfree (%)	16.4 / 23.4

The structure of Crystal Structure of D157A Mutant of Pseudomonas Sp. MIS38 Lipase also contains other interesting chemical elements:

Calcium

(Ca)

10 atoms

The binding sites of Zinc atom in the Crystal Structure of D157A Mutant of Pseudomonas Sp. MIS38 Lipase (pdb code 2zj7). 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 D157A Mutant of Pseudomonas Sp. MIS38 Lipase, PDB code: 2zj7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of D157A Mutant of Pseudomonas Sp. MIS38 Lipase


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 D157A Mutant of Pseudomonas Sp. MIS38 Lipase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn628 b:0.0 occ:1.00 ND1 A:HIS132 2.2 28.4 1.0 CE1 A:HIS132 2.6 21.6 1.0 OD2 A:ASP128 3.3 27.8 1.0 CG A:HIS132 3.5 24.3 1.0 CB A:GLN130 3.7 29.5 1.0 OD1 A:ASP128 3.8 22.3 1.0 CG A:GLN130 3.8 31.3 1.0 CG A:ASP128 3.8 24.9 1.0 NE2 A:HIS132 3.9 27.4 1.0 CB A:HIS132 4.3 24.9 1.0 CD2 A:HIS132 4.3 23.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of D157A Mutant of Pseudomonas Sp. MIS38 Lipase


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 D157A Mutant of Pseudomonas Sp. MIS38 Lipase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn629 b:31.4 occ:1.00 OE2 A:GLU537 2.0 34.2 1.0 NE2 A:HIS517 2.3 21.1 1.0 CD A:GLU537 3.0 34.3 1.0 OE1 A:GLU537 3.2 37.4 1.0 CE1 A:HIS517 3.2 29.1 1.0 CD2 A:HIS517 3.2 24.1 1.0 CG1 A:ILE519 4.3 24.2 1.0 CG A:GLU537 4.3 29.5 1.0 ND1 A:HIS517 4.3 28.7 1.0 CG A:HIS517 4.4 24.5 1.0 CD1 A:ILE519 4.6 27.8 1.0 CD2 A:LEU535 4.8 27.2 1.0

K.Kuwahara, C.Angkawidjaja, H.Matsumura, Y.Koga, K.Takano, S.Kanaya. Importance of the CA2+-Binding Sites in the N-Catalytic Domain of A Family I.3 Lipase For Activity and Stability Protein Eng.Des.Sel. V. 21 737 2008.
ISSN: ISSN 1741-0126
PubMed: 18987131
DOI: 10.1093/PROTEIN/GZN057