Zinc in PDB 6htm: X-Ray Structure of the Tryptophan Lyase Nosl in Complex with Bound Tryptamin

The structure of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with Bound Tryptamin, PDB code: 6htm was solved by P.Amara, J.M.Mouesca, M.Bella, C.Saragaglia, S.Gambarelli, Y.Nicolet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.05 / 1.70
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.530, 47.140, 113.900, 90.00, 108.90, 90.00
R / Rfree (%)	16.2 / 18.9

The structure of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with Bound Tryptamin also contains other interesting chemical elements:

Bromine	(Br)	6 atoms
Iron	(Fe)	8 atoms
Chlorine	(Cl)	7 atoms

The binding sites of Zinc atom in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with Bound Tryptamin (pdb code 6htm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with Bound Tryptamin, PDB code: 6htm:

Zinc binding site 1 out of 1 in the X-Ray Structure of the Tryptophan Lyase Nosl in Complex with Bound Tryptamin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of the Tryptophan Lyase Nosl in Complex with Bound Tryptamin within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn515 b:31.6 occ:0.70 OE1 B:GLU126 2.0 38.5 1.0 NE2 B:HIS130 2.0 29.0 1.0 CL B:CL514 2.2 48.2 0.7 O B:HOH968 2.5 56.9 1.0 CD B:GLU126 2.8 34.4 1.0 CD2 B:HIS130 2.8 24.9 1.0 OE2 B:GLU126 3.0 39.3 1.0 CE1 B:HIS130 3.1 29.6 1.0 O B:HOH771 4.0 46.1 0.3 CG B:HIS130 4.0 25.5 1.0 ND1 B:HIS130 4.1 27.4 1.0 CG B:GLU126 4.2 23.1 1.0 CB B:GLU126 4.6 21.4 1.0 CD1 B:TYR129 4.9 21.9 1.0

P.Amara, J.M.Mouesca, M.Bella, L.Martin, C.Saragaglia, S.Gambarelli, Y.Nicolet. Radical S-Adenosyl-L-Methionine Tryptophan Lyase (Nosl): How the Protein Controls the Carboxyl Radical •CO2-Migration. J.Am.Chem.Soc. V. 140 16661 2018.
ISSN: ESSN 1520-5126
PubMed: 30418774
DOI: 10.1021/JACS.8B09142