Manganese in PDB 1ybu: Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog.

All present enzymatic activity of Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog.:
4.6.1.1;

The structure of Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog., PDB code: 1ybu was solved by S.C.Sinha, M.Wetterer, S.R.Sprang, J.E.Schultz, J.U.Linder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.94 / 2.40
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.067, 48.923, 68.198, 90.00, 90.00, 90.00
R / Rfree (%)	23.3 / 26.2

The binding sites of Manganese atom in the Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog. (pdb code 1ybu). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog., PDB code: 1ybu:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:0.6 occ:1.00 O2A A:APC601 2.3 0.2 1.0 PA A:APC601 2.4 0.2 1.0 O1A A:APC601 2.5 0.9 1.0 OG A:SER306 2.6 37.1 1.0 O A:HOH3 2.7 28.6 1.0 O A:ILE303 2.8 27.1 1.0 OD1 A:ASP302 2.9 48.8 1.0 OD2 A:ASP346 3.1 76.9 1.0 C3A A:APC601 3.2 96.7 1.0 O3B A:APC601 3.3 95.1 1.0 CB A:SER306 3.5 29.6 1.0 OD2 A:ASP302 3.6 46.1 1.0 CG A:ASP302 3.6 45.0 1.0 N A:SER306 3.8 27.6 1.0 C A:ILE303 4.0 24.0 1.0 O5' A:APC601 4.0 94.1 1.0 PB A:APC601 4.0 96.2 1.0 CG A:ASP346 4.1 72.7 1.0 CA A:SER306 4.3 34.5 1.0 OD1 A:ASP346 4.4 73.3 1.0 O A:HOH223 4.4 53.9 1.0 N A:GLY305 4.5 31.2 1.0 O2B A:APC601 4.5 93.0 1.0 PG A:APC601 4.6 99.2 1.0 C5' A:APC601 4.6 85.6 1.0 O2G A:APC601 4.7 96.5 1.0 N A:THR307 4.8 38.6 1.0 N A:ILE303 4.8 31.1 1.0 CA A:VAL304 4.9 28.5 1.0 N A:VAL304 4.9 26.3 1.0 NH1 A:ARG377 4.9 56.0 1.0 CA A:ILE303 4.9 25.4 1.0 C A:VAL304 4.9 29.5 1.0 C A:GLY305 4.9 30.6 1.0

Manganese binding site 2 out of 2 in the Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Mycobacterium Tuberculosis Adenylyl Cyclase RV1900C Chd, in Complex with A Substrate Analog. within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn502 b:0.3 occ:1.00 O2A D:APC602 2.3 0.9 1.0 PA D:APC602 2.4 0.5 1.0 O1A D:APC602 2.5 0.6 1.0 OG D:SER306 2.7 36.3 1.0 O D:ILE303 2.7 26.7 1.0 OD1 D:ASP302 3.0 43.2 1.0 OD2 D:ASP346 3.1 77.4 1.0 C3A D:APC602 3.2 98.0 1.0 O3B D:APC602 3.3 95.6 1.0 CB D:SER306 3.5 25.2 1.0 CG D:ASP302 3.8 41.8 1.0 OD2 D:ASP302 3.8 42.5 1.0 N D:SER306 3.9 21.4 1.0 C D:ILE303 4.0 21.8 1.0 O5' D:APC602 4.0 93.5 1.0 PB D:APC602 4.0 98.8 1.0 CG D:ASP346 4.1 74.0 1.0 CA D:SER306 4.3 32.2 1.0 OD1 D:ASP346 4.4 73.6 1.0 N D:GLY305 4.4 30.6 1.0 O2B D:APC602 4.5 95.1 1.0 PG D:APC602 4.6 97.9 1.0 O D:HOH224 4.6 62.9 1.0 C5' D:APC602 4.6 86.2 1.0 O2G D:APC602 4.7 96.5 1.0 N D:ILE303 4.7 30.2 1.0 N D:THR307 4.8 36.9 1.0 CA D:ILE303 4.8 23.7 1.0 CA D:VAL304 4.9 26.8 1.0 N D:VAL304 4.9 23.7 1.0 C D:VAL304 4.9 29.0 1.0 C D:GLY305 5.0 27.7 1.0

S.C.Sinha, M.Wetterer, S.R.Sprang, J.E.Schultz, J.U.Linder. Origin of Asymmetry in Adenylyl Cyclases: Structures of Mycobacterium Tuberculosis RV1900C. Embo J. V. 24 663 2005.
ISSN: ISSN 0261-4189
PubMed: 15678099
DOI: 10.1038/SJ.EMBOJ.7600573