Manganese in PDB 2w1a: Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa

All present enzymatic activity of Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa:
2.5.1.54; 5.4.99.5;

The structure of Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa, PDB code: 2w1a was solved by M.Okvist, S.Sasso, K.Roderer, M.Gamper, G.Codoni, U.Krengel, P.Kast, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.84 / 2.35
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	205.910, 205.910, 67.240, 90.00, 90.00, 120.00
R / Rfree (%)	19.057 / 22.918

The binding sites of Manganese atom in the Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa (pdb code 2w1a). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa, PDB code: 2w1a:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1463 b:33.1 occ:1.00 OE1 A:GLU411 2.2 29.4 1.0 OD2 A:ASP441 2.3 35.5 1.0 NE2 A:HIS369 2.4 28.1 1.0 SG A:CYS87 2.5 28.9 1.0 OE2 A:GLU411 2.8 31.0 1.0 CD A:GLU411 2.9 29.6 1.0 CG A:ASP441 3.3 35.3 1.0 CE1 A:HIS369 3.3 28.7 1.0 CD2 A:HIS369 3.4 28.2 1.0 CB A:CYS87 3.5 28.1 1.0 CB A:ASP441 3.5 35.4 1.0 CA A:CYS87 4.1 28.0 1.0 NH2 A:ARG126 4.2 24.1 1.0 O A:HOH2027 4.3 30.8 1.0 NH2 A:ARG382 4.3 37.3 1.0 CG A:GLU411 4.3 29.1 1.0 OD1 A:ASP441 4.4 35.2 1.0 ND1 A:HIS369 4.5 28.3 1.0 CG A:HIS369 4.5 28.9 1.0 CA A:ASP441 4.7 35.3 1.0 N A:ASP441 4.8 34.7 1.0 C A:CYS87 4.8 28.1 1.0 O A:CYS87 4.8 28.1 1.0 CZ A:ARG126 4.9 25.9 1.0

Manganese binding site 2 out of 2 in the Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Non-Covalent Complex Between Dahp Synthase and Chorismate Mutase From Mycobacterium Tuberculosis with Bound Tsa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1465 b:38.9 occ:1.00 OE1 B:GLU411 2.3 32.9 1.0 NE2 B:HIS369 2.4 27.2 1.0 OD2 B:ASP441 2.5 39.2 1.0 SG B:CYS87 2.6 33.0 1.0 OE2 B:GLU411 2.9 30.8 1.0 CD B:GLU411 2.9 29.2 1.0 CE1 B:HIS369 3.3 27.2 1.0 CG B:ASP441 3.4 41.6 1.0 CD2 B:HIS369 3.5 28.6 1.0 CB B:ASP441 3.6 42.2 1.0 CB B:CYS87 3.7 29.5 1.0 NH2 B:ARG382 4.1 43.1 1.0 NH2 B:ARG126 4.2 23.2 1.0 O B:HOH2104 4.3 32.6 1.0 CA B:CYS87 4.3 29.4 1.0 CG B:GLU411 4.4 29.7 1.0 ND1 B:HIS369 4.4 29.3 1.0 CG B:HIS369 4.6 28.9 1.0 OD1 B:ASP441 4.6 42.6 1.0 O B:CYS87 4.8 29.1 1.0 CZ B:ARG126 4.9 24.7 1.0 C B:CYS87 4.9 28.7 1.0 NH1 B:ARG126 4.9 25.7 1.0 CA B:ASP441 4.9 42.0 1.0 NH1 B:ARG382 4.9 44.8 1.0

S.Sasso, M.Okvist, K.Roderer, M.Gamper, G.Codoni, U.Krengel, P.Kast. Structure and Function of A Complex Between Chorismate Mutase and Dahp Synthase: Efficiency Boost For the Junior Partner. Embo J. V. 28 2128 2009.
ISSN: ISSN 0261-4189
PubMed: 19556970
DOI: 10.1038/EMBOJ.2009.165