Manganese in PDB 5ckv: Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan

All present enzymatic activity of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan:
2.5.1.54;

The structure of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan, PDB code: 5ckv was solved by S.Munack, U.Krengel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.30 / 2.79
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	204.760, 204.760, 66.774, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 22.6

The structure of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Manganese atom in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan (pdb code 5ckv). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan, PDB code: 5ckv:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and 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 Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn508 b:65.1 occ:1.00 OE2 A:GLU411 2.1 53.0 1.0 OD2 A:ASP441 2.1 71.1 1.0 NE2 A:HIS369 2.2 58.7 1.0 O A:HOH604 2.3 64.5 1.0 SG A:CYS87 2.7 55.9 1.0 CD A:GLU411 3.0 55.2 1.0 HB2 A:ASP441 3.0 64.1 1.0 CD2 A:HIS369 3.1 64.6 1.0 HD2 A:HIS369 3.1 77.5 1.0 CG A:ASP441 3.1 56.5 1.0 OE1 A:GLU411 3.2 61.1 1.0 CE1 A:HIS369 3.2 64.6 1.0 HE1 A:HIS369 3.5 77.6 1.0 CB A:ASP441 3.6 53.4 1.0 HH12 A:ARG382 3.6 79.3 1.0 HB2 A:CYS87 3.7 70.2 1.0 HH22 A:ARG126 3.8 60.5 1.0 CB A:CYS87 3.9 58.5 1.0 HB3 A:ASP441 4.0 64.1 1.0 HA A:CYS87 4.1 50.9 1.0 OD1 A:ASP441 4.2 65.8 1.0 NH2 A:ARG126 4.2 50.4 1.0 CG A:HIS369 4.2 67.9 1.0 ND1 A:HIS369 4.3 74.8 1.0 H A:ASP441 4.3 54.8 1.0 HG A:CYS440 4.3 0.6 1.0 HH22 A:ARG382 4.3 67.7 1.0 HH21 A:ARG126 4.4 60.5 1.0 CG A:GLU411 4.4 51.3 1.0 NH1 A:ARG382 4.5 66.1 1.0 CA A:CYS87 4.5 42.4 1.0 HG2 A:GLU411 4.6 61.6 1.0 HB3 A:CYS87 4.6 70.2 1.0 HG3 A:GLU411 4.8 61.6 1.0 CA A:ASP441 4.9 53.2 1.0 HH12 A:ARG126 4.9 76.4 1.0 O A:CYS87 4.9 47.5 1.0 N A:ASP441 4.9 45.7 1.0 SG A:CYS440 4.9 84.6 1.0 HH11 A:ARG382 5.0 79.3 1.0

Manganese binding site 2 out of 2 in the Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Dahp Synthase From Mycobacterium Tuberculosis, Fully Inhibited By Tyrosine, Phenylalanine, and Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:59.1 occ:0.83 OE2 B:GLU411 2.1 50.8 1.0 NE2 B:HIS369 2.2 50.5 1.0 OD2 B:ASP441 2.2 62.1 1.0 SG B:CYS87 2.6 59.0 1.0 CD B:GLU411 2.9 59.6 1.0 HB2 B:ASP441 2.9 64.7 1.0 CE1 B:HIS369 3.0 44.0 1.0 OE1 B:GLU411 3.0 57.8 1.0 HE1 B:HIS369 3.1 52.8 1.0 CG B:ASP441 3.2 60.4 1.0 HH22 B:ARG382 3.2 57.8 1.0 CD2 B:HIS369 3.3 52.5 1.0 CB B:ASP441 3.5 53.9 1.0 HD2 B:HIS369 3.5 63.0 1.0 HB2 B:CYS87 3.7 67.9 1.0 CB B:CYS87 3.8 56.6 1.0 HH22 B:ARG126 3.8 58.7 1.0 HB3 B:ASP441 3.9 64.7 1.0 NH2 B:ARG382 4.0 48.2 1.0 HA B:CYS87 4.1 53.8 1.0 ND1 B:HIS369 4.2 47.9 1.0 OD1 B:ASP441 4.3 64.0 1.0 HH12 B:ARG382 4.3 66.6 1.0 NH2 B:ARG126 4.3 48.9 1.0 CG B:HIS369 4.3 53.1 1.0 CG B:GLU411 4.3 54.5 1.0 H B:ASP441 4.4 55.8 1.0 HH21 B:ARG382 4.4 57.8 1.0 CA B:CYS87 4.5 44.8 1.0 HG2 B:GLU411 4.5 65.4 1.0 HB3 B:CYS87 4.6 67.9 1.0 HH21 B:ARG126 4.6 58.7 1.0 HG3 B:GLU411 4.7 65.4 1.0 HH12 B:ARG126 4.7 56.5 1.0 CA B:ASP441 4.8 52.4 1.0 N B:ASP441 4.9 46.5 1.0 HD1 B:HIS369 4.9 57.5 1.0 NH1 B:ARG382 5.0 55.5 1.0 CZ B:ARG382 5.0 54.7 1.0

S.Munack, K.Roderer, M.Okvist, J.Kamarauskaite, S.Sasso, A.Van Eerde, P.Kast, U.Krengel. Remote Control By Inter-Enzyme Allostery: A Novel Paradigm For Regulation of the Shikimate Pathway. J.Mol.Biol. V. 428 1237 2016.
ISSN: ESSN 1089-8638
PubMed: 26776476
DOI: 10.1016/J.JMB.2016.01.001