Zinc in PDB 8d19: Human LANCL1 Bound to Gsh

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

The structure of Human LANCL1 Bound to Gsh, PDB code: 8d19 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 / 1.52
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.505, 121.134, 142.895, 90, 90, 90
R / Rfree (%)	17.2 / 19.2

The binding sites of Zinc atom in the Human LANCL1 Bound to Gsh (pdb code 8d19). 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 Bound to Gsh, PDB code: 8d19:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human LANCL1 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 Bound to Gsh within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:15.1 occ:1.00 ND1 A:HIS323 2.1 14.0 1.0 SG A:CYS276 2.3 14.5 1.0 SG A:CYS322 2.3 13.5 1.0 SG2 A:GSH501 2.4 16.1 1.0 CE1 A:HIS323 2.9 14.6 1.0 CB A:CYS276 3.1 13.8 1.0 CG A:HIS323 3.2 14.4 1.0 CB2 A:GSH501 3.2 16.4 1.0 CB A:CYS322 3.4 12.9 1.0 O A:CYS322 3.6 13.2 1.0 CA2 A:GSH501 3.6 17.5 1.0 CB A:HIS323 3.6 14.4 1.0 C A:CYS322 3.7 13.4 1.0 OH A:TYR62 3.9 17.5 1.0 N A:HIS323 4.1 13.5 1.0 CA A:CYS322 4.1 12.9 1.0 NE2 A:HIS323 4.1 14.9 1.0 CD2 A:HIS323 4.2 14.9 1.0 CA A:CYS276 4.4 13.8 1.0 CA A:HIS323 4.4 14.0 1.0 N2 A:GSH501 4.5 17.2 1.0 N A:CYS276 4.6 13.5 1.0 O2 A:GSH501 4.7 18.7 1.0 C2 A:GSH501 4.7 18.4 1.0 O A:HOH661 4.8 25.5 1.0 ND1 A:HIS274 4.8 16.1 1.0

Zinc binding site 2 out of 2 in the Human LANCL1 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 Bound to Gsh within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn500 b:15.4 occ:1.00 ND1 B:HIS323 2.1 13.9 1.0 SG B:CYS322 2.3 13.9 1.0 SG B:CYS276 2.3 14.6 1.0 SG2 B:GSH501 2.4 17.2 1.0 CE1 B:HIS323 2.9 14.4 1.0 CB B:CYS276 3.1 14.1 1.0 CG B:HIS323 3.2 14.5 1.0 CB2 B:GSH501 3.2 17.2 1.0 CB B:CYS322 3.3 13.0 1.0 O B:CYS322 3.6 13.7 1.0 C B:CYS322 3.6 13.8 1.0 CB B:HIS323 3.7 14.8 1.0 CA2 B:GSH501 3.7 18.1 1.0 OH B:TYR62 3.9 17.9 1.0 N B:HIS323 4.0 14.0 1.0 CA B:CYS322 4.1 13.1 1.0 NE2 B:HIS323 4.1 14.9 1.0 CD2 B:HIS323 4.3 14.7 1.0 CA B:CYS276 4.4 14.0 1.0 CA B:HIS323 4.4 14.2 1.0 N2 B:GSH501 4.5 17.5 1.0 N B:CYS276 4.6 13.8 1.0 O2 B:GSH501 4.7 18.3 1.0 O B:HOH632 4.7 26.1 1.0 C2 B:GSH501 4.7 18.8 1.0 ND1 B:HIS274 4.8 16.0 1.0 O B:HOH789 5.0 30.7 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