Zinc in PDB 2z5g: Crystal Structure of T1 Lipase F16L Mutant

All present enzymatic activity of Crystal Structure of T1 Lipase F16L Mutant:
3.1.1.3;

The structure of Crystal Structure of T1 Lipase F16L Mutant, PDB code: 2z5g was solved by H.Matsumura, T.Yamamoto, T.Inoue, Y.Kai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.25 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	117.784, 81.111, 99.475, 90.00, 96.90, 90.00
R / Rfree (%)	19.6 / 21.2

The structure of Crystal Structure of T1 Lipase F16L Mutant also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Calcium	(Ca)	2 atoms

The binding sites of Zinc atom in the Crystal Structure of T1 Lipase F16L Mutant (pdb code 2z5g). 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 T1 Lipase F16L Mutant, PDB code: 2z5g:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of T1 Lipase F16L Mutant


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 T1 Lipase F16L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2001 b:21.3 occ:1.00 OD2 A:ASP238 2.0 10.6 1.0 NE2 A:HIS81 2.1 12.4 1.0 OD1 A:ASP61 2.1 10.8 1.0 NE2 A:HIS87 2.2 12.2 1.0 OD2 A:ASP61 2.6 12.1 1.0 CG A:ASP238 2.7 12.6 1.0 CG A:ASP61 2.7 11.9 1.0 OD1 A:ASP238 2.7 13.4 1.0 CD2 A:HIS81 3.0 14.4 1.0 CE1 A:HIS81 3.1 15.4 1.0 CD2 A:HIS87 3.1 11.5 1.0 CE1 A:HIS87 3.3 11.2 1.0 OG A:SER58 3.9 12.8 1.0 CB A:ASP238 4.1 13.1 1.0 CB A:ASP61 4.1 10.4 1.0 CG A:HIS81 4.2 14.9 1.0 ND1 A:HIS81 4.2 14.4 1.0 O A:HOH2228 4.3 16.2 1.0 CG A:HIS87 4.3 13.1 1.0 ND1 A:HIS87 4.3 11.9 1.0 CD1 A:TRP60 4.5 13.3 1.0 CD2 A:HIS85 4.7 14.9 1.0 CA A:ASP61 4.8 11.2 1.0 N A:ASP61 4.8 10.3 1.0 O A:ASP238 4.9 12.2 1.0 CD1 A:TYR77 4.9 10.0 1.0 CB A:HIS85 5.0 13.6 1.0 CZ2 A:TRP211 5.0 17.1 1.0 CG A:HIS85 5.0 15.2 1.0 CB A:SER58 5.0 14.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of T1 Lipase F16L Mutant


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 T1 Lipase F16L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2002 b:19.9 occ:1.00 OD2 B:ASP238 2.1 12.9 1.0 NE2 B:HIS81 2.1 14.0 1.0 OD1 B:ASP61 2.1 16.7 1.0 NE2 B:HIS87 2.3 16.4 1.0 OD2 B:ASP61 2.7 14.0 1.0 CG B:ASP238 2.7 15.3 1.0 CG B:ASP61 2.7 15.8 1.0 OD1 B:ASP238 2.7 14.1 1.0 CD2 B:HIS81 3.0 14.6 1.0 CE1 B:HIS81 3.1 14.7 1.0 CD2 B:HIS87 3.1 16.0 1.0 CE1 B:HIS87 3.3 17.7 1.0 OG B:SER58 3.8 16.2 1.0 CB B:ASP238 4.1 13.3 1.0 CB B:ASP61 4.2 14.5 1.0 ND1 B:HIS81 4.2 14.4 1.0 CG B:HIS81 4.2 14.6 1.0 O B:HOH2213 4.3 14.7 1.0 CG B:HIS87 4.3 17.0 1.0 ND1 B:HIS87 4.4 16.4 1.0 CD1 B:TRP60 4.6 13.3 1.0 CD2 B:HIS85 4.7 18.2 1.0 CA B:ASP61 4.8 14.0 1.0 N B:ASP61 4.9 13.2 1.0 O B:ASP238 4.9 13.9 1.0 CB B:SER58 4.9 14.9 1.0 CB B:HIS85 4.9 16.7 1.0 CG B:HIS85 5.0 18.7 1.0 CD1 B:TYR77 5.0 13.4 1.0

H.Matsumura, T.Yamamoto, T.C.Leow, T.Mori, A.B.Salleh, M.Basri, T.Inoue, Y.Kai, R.N.Z.R.A.Rahman. Novel Cation-Pi Interaction Revealed By Crystal Structure of Thermoalkalophilic Lipase Proteins V. 70 592 2007.
ISSN: ISSN 0887-3585
PubMed: 17932933
DOI: 10.1002/PROT.21799