Zinc in PDB 7ey3: Double Cysteine Mutations in T1 Lipase

All present enzymatic activity of Double Cysteine Mutations in T1 Lipase:
3.1.1.3;

The structure of Double Cysteine Mutations in T1 Lipase, PDB code: 7ey3 was solved by S.H.Hamdan, T.C.Leow, N.M.Yahaya, M.S.M.Ali, M.A.Jonet, S.N.A.Mohamadaris, J.Maiangwa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.46 / 2.04
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.174, 81.496, 100.046, 90, 96.94, 90
R / Rfree (%)	18.8 / 22.2

The structure of Double Cysteine Mutations in T1 Lipase also contains other interesting chemical elements:

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

The binding sites of Zinc atom in the Double Cysteine Mutations in T1 Lipase (pdb code 7ey3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Double Cysteine Mutations in T1 Lipase, PDB code: 7ey3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Double Cysteine Mutations in T1 Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Double Cysteine Mutations in T1 Lipase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2001 b:22.0 occ:1.00 OD2 A:ASP238 2.0 12.8 1.0 OD1 A:ASP61 2.1 12.7 1.0 NE2 A:HIS87 2.2 13.9 1.0 NE2 A:HIS81 2.2 12.6 1.0 OD2 A:ASP61 2.7 12.9 1.0 CG A:ASP61 2.7 14.9 1.0 CG A:ASP238 2.8 14.7 1.0 OD1 A:ASP238 2.9 14.6 1.0 CD2 A:HIS81 3.0 14.0 1.0 CD2 A:HIS87 3.1 15.2 1.0 CE1 A:HIS87 3.3 9.2 1.0 CE1 A:HIS81 3.4 15.0 1.0 OG A:SER58 3.9 13.7 1.0 O A:HOH2116 4.2 13.3 1.0 CB A:ASP238 4.2 11.4 1.0 CB A:ASP61 4.2 10.4 1.0 CG A:HIS81 4.2 16.0 1.0 CG A:HIS87 4.3 11.6 1.0 ND1 A:HIS87 4.4 17.1 1.0 ND1 A:HIS81 4.4 15.0 1.0 CD1 A:TRP60 4.5 11.1 1.0 CD2 A:HIS85 4.7 18.6 1.0 N A:ASP61 4.8 10.3 1.0 CA A:ASP61 4.8 9.7 1.0 O A:ASP238 4.9 15.6 1.0 CB A:SER58 5.0 11.7 1.0

Zinc binding site 2 out of 2 in the Double Cysteine Mutations in T1 Lipase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Double Cysteine Mutations in T1 Lipase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:24.7 occ:1.00 OD2 B:ASP238 2.0 18.3 1.0 OD1 B:ASP61 2.1 17.2 1.0 NE2 B:HIS81 2.2 12.7 1.0 NE2 B:HIS87 2.3 17.8 1.0 CG B:ASP61 2.7 17.3 1.0 OD2 B:ASP61 2.7 16.5 1.0 CG B:ASP238 2.8 18.6 1.0 OD1 B:ASP238 2.9 13.6 1.0 CD2 B:HIS87 3.0 16.9 1.0 CD2 B:HIS81 3.0 15.7 1.0 CE1 B:HIS81 3.3 15.0 1.0 CE1 B:HIS87 3.4 18.5 1.0 OG B:SER58 3.8 15.4 1.0 CB B:ASP61 4.2 11.1 1.0 O B:HOH523 4.2 17.1 1.0 CB B:ASP238 4.2 14.7 1.0 CG B:HIS81 4.2 14.7 1.0 CG B:HIS87 4.3 16.0 1.0 ND1 B:HIS81 4.3 20.8 1.0 ND1 B:HIS87 4.4 18.7 1.0 CD1 B:TRP60 4.5 13.7 1.0 ND1 B:HIS85 4.8 20.5 1.0 N B:ASP61 4.8 14.7 1.0 CA B:ASP61 4.8 13.8 1.0 CB B:SER58 4.9 15.2 1.0 O B:ASP238 4.9 16.3 1.0

S.H.Hamdan, T.C.Leow. Double Cysteine Mutations in T1 Lipase To Be Published.