Zinc in PDB 8d0v: Human LANCL1 C264A Mutant Bound to Gsh

All present enzymatic activity of Human LANCL1 C264A Mutant Bound to Gsh:
2.5.1.18;

The structure of Human LANCL1 C264A Mutant Bound to Gsh, PDB code: 8d0v was solved by C.Ongpipattanakul, S.K.Nair, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.587, 120.257, 143.019, 90, 90, 90
R / Rfree (%)	18.1 / 20.2

The binding sites of Zinc atom in the Human LANCL1 C264A Mutant Bound to Gsh (pdb code 8d0v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human LANCL1 C264A Mutant Bound to Gsh, PDB code: 8d0v:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human LANCL1 C264A Mutant Bound to Gsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human LANCL1 C264A Mutant Bound to Gsh within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:23.8 occ:1.00 ND1 A:HIS323 2.1 21.8 1.0 SG A:CYS276 2.3 23.7 1.0 SG A:CYS322 2.3 20.8 1.0 SG2 A:GSH501 2.4 23.9 1.0 CE1 A:HIS323 3.0 22.7 1.0 CB A:CYS276 3.1 21.6 1.0 CG A:HIS323 3.2 23.4 1.0 CB2 A:GSH501 3.2 23.3 1.0 CB A:CYS322 3.4 19.2 1.0 O A:CYS322 3.5 19.6 1.0 CB A:HIS323 3.6 22.3 1.0 C A:CYS322 3.6 20.5 1.0 CA2 A:GSH501 3.6 25.4 1.0 OH A:TYR62 4.0 23.8 1.0 N A:HIS323 4.0 20.7 1.0 CA A:CYS322 4.0 18.8 1.0 NE2 A:HIS323 4.1 24.9 1.0 CD2 A:HIS323 4.2 24.1 1.0 CA A:HIS323 4.4 21.5 1.0 CA A:CYS276 4.4 21.5 1.0 N2 A:GSH501 4.5 24.1 1.0 N A:CYS276 4.6 20.4 1.0 O2 A:GSH501 4.7 26.2 1.0 C2 A:GSH501 4.7 25.9 1.0 ND1 A:HIS274 4.8 25.4 1.0

Zinc binding site 2 out of 2 in the Human LANCL1 C264A Mutant Bound to Gsh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human LANCL1 C264A Mutant Bound to Gsh within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn500 b:23.8 occ:1.00 ND1 B:HIS323 2.0 20.1 1.0 SG B:CYS276 2.3 24.0 1.0 SG B:CYS322 2.3 21.3 1.0 SG2 B:GSH501 2.4 24.6 1.0 CE1 B:HIS323 2.9 20.7 1.0 CB B:CYS276 3.1 22.2 1.0 CG B:HIS323 3.2 21.1 1.0 CB2 B:GSH501 3.2 23.6 1.0 CB B:CYS322 3.4 18.6 1.0 O B:CYS322 3.5 20.0 1.0 CA2 B:GSH501 3.6 24.5 1.0 CB B:HIS323 3.6 19.5 1.0 C B:CYS322 3.6 21.3 1.0 OH B:TYR62 4.0 24.9 1.0 N B:HIS323 4.0 20.5 1.0 CA B:CYS322 4.1 20.3 1.0 NE2 B:HIS323 4.1 22.7 1.0 CD2 B:HIS323 4.2 20.5 1.0 CA B:HIS323 4.4 20.8 1.0 CA B:CYS276 4.4 21.8 1.0 N2 B:GSH501 4.5 23.1 1.0 N B:CYS276 4.6 20.5 1.0 O2 B:GSH501 4.7 27.3 1.0 C2 B:GSH501 4.7 26.5 1.0 ND1 B:HIS274 4.7 25.4 1.0 O B:HOH612 4.8 29.8 1.0

C.Ongpipattanakul, S.Liu, Y.Luo, S.K.Nair, W.A.Van Der Donk. The Mechanism of Thia-Michael Addition Catalyzed By Lanc Enzymes. Proc.Natl.Acad.Sci.Usa V. 120 23120 2023.
ISSN: ESSN 1091-6490
PubMed: 36634136
DOI: 10.1073/PNAS.2217523120