Manganese in PDB 5hue: Dahp Synthase From Corynebacterium Glutamicum in Complex with Tryptophan

The structure of Dahp Synthase From Corynebacterium Glutamicum in Complex with Tryptophan, PDB code: 5hue was solved by D.Burschowsky, J.B.Heim, H.V.Thorbjoernsrud, U.Krengel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.01 / 2.65
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	109.189, 109.189, 279.897, 90.00, 90.00, 120.00
R / Rfree (%)	24.7 / 28.5

The binding sites of Manganese atom in the Dahp Synthase From Corynebacterium Glutamicum in Complex with Tryptophan (pdb code 5hue). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Dahp Synthase From Corynebacterium Glutamicum in Complex with Tryptophan, PDB code: 5hue:

Manganese binding site 1 out of 1 in the Dahp Synthase From Corynebacterium Glutamicum in Complex with Tryptophan


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Dahp Synthase From Corynebacterium Glutamicum in Complex with Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:0.3 occ:0.92 OD2 A:ASP451 1.9 0.4 1.0 OE2 A:GLU421 1.9 0.0 1.0 NE2 A:HIS379 2.0 0.2 1.0 SG A:CYS97 2.3 0.4 0.7 CD A:GLU421 2.7 1.0 1.0 CG A:ASP451 2.9 0.3 1.0 CE1 A:HIS379 2.9 0.8 1.0 OE1 A:GLU421 2.9 0.1 1.0 CD2 A:HIS379 3.0 0.0 1.0 O2' A:PEP502 3.3 0.9 1.0 CB A:ASP451 3.3 0.7 1.0 CB A:CYS97 3.5 0.8 1.0 O1 A:PEP502 3.8 1.0 1.0 C1 A:PEP502 3.9 0.9 1.0 OD1 A:ASP451 3.9 0.9 1.0 ND1 A:HIS379 4.0 0.9 1.0 NH2 A:ARG392 4.1 0.5 1.0 CG A:HIS379 4.1 0.2 1.0 CA A:CYS97 4.2 0.9 1.0 CG A:GLU421 4.2 99.5 1.0 NH2 A:ARG136 4.2 96.0 1.0 CA A:ASP451 4.6 0.2 1.0 CE A:LYS143 4.6 0.2 1.0 NH1 A:ARG136 4.7 98.9 1.0 NZ A:LYS143 4.7 0.5 1.0 CZ A:ARG136 4.7 95.1 1.0 N A:ASP451 4.7 0.7 1.0 O A:CYS97 4.8 0.2 1.0 C A:CYS97 4.8 0.2 1.0 NH1 A:ARG392 4.9 0.3 1.0 CZ A:ARG392 5.0 1.0 1.0

D.Burschowsky, H.V.Thorbjornsrud, J.B.Heim, J.R.Fahrig-Kamarauskaite, K.Wurth-Roderer, P.Kast, U.Krengel. Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium Glutamicum: Structural Basis of Feedback Activation By Trp. Biochemistry V. 57 557 2018.
ISSN: ISSN 1520-4995
PubMed: 29178787
DOI: 10.1021/ACS.BIOCHEM.7B01018