Manganese in PDB 1mqw: Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme

All present enzymatic activity of Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme:
3.6.1.13;

The structure of Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme, PDB code: 1mqw was solved by L.-W.Kang, S.B.Gabelli, M.A.Bianchet, J.E.Cunningham, S.F.O'handley, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	64.078, 64.078, 182.887, 90.00, 90.00, 120.00
R / Rfree (%)	20.5 / 26.6

The binding sites of Manganese atom in the Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme (pdb code 1mqw). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme, PDB code: 1mqw:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:40.7 occ:1.00 OR5 A:ADV301 2.1 41.0 1.0 O2A A:ADV301 2.1 53.9 1.0 O A:HOH412 2.1 41.6 1.0 O A:ALA76 2.1 33.9 1.0 O A:HOH406 2.1 41.2 1.0 OE2 A:GLU97 2.1 41.1 1.0 CX A:ADV301 3.1 51.3 1.0 PB A:ADV301 3.1 44.3 1.0 PA A:ADV301 3.2 56.1 1.0 CD A:GLU97 3.2 40.6 1.0 MN A:MN402 3.3 55.3 1.0 C A:ALA76 3.3 30.8 1.0 OE1 A:GLU97 3.7 41.3 1.0 OE2 A:GLU142 4.0 60.1 1.0 O1B A:ADV301 4.1 42.8 1.0 N A:ALA76 4.2 28.7 1.0 N A:GLY77 4.2 29.9 1.0 OE1 A:GLN62 4.2 30.3 1.0 O2B A:ADV301 4.2 41.8 1.0 CA A:GLY77 4.2 31.1 1.0 CA A:ALA76 4.3 29.7 1.0 O5' A:ADV301 4.3 57.9 1.0 OE1 A:GLU93 4.3 48.0 1.0 O1A A:ADV301 4.4 56.9 1.0 O A:HOH408 4.4 25.9 1.0 C5' A:ADV301 4.4 61.9 1.0 NE2 A:GLN62 4.5 29.6 1.0 CG A:GLU97 4.5 39.5 1.0 CD A:GLU142 4.8 61.8 1.0 CB A:ALA76 4.8 30.2 1.0 CD A:GLN62 4.8 30.3 1.0 O A:HOH407 4.9 59.2 1.0 O A:HOH413 5.0 55.3 1.0

Manganese binding site 2 out of 3 in the Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:55.3 occ:1.00 O2A A:ADV301 2.1 53.9 1.0 OE1 A:GLU93 2.1 48.0 1.0 OE2 A:GLU142 2.1 60.1 1.0 O A:HOH407 2.2 59.2 1.0 OE2 A:GLU97 2.7 41.1 1.0 CD A:GLU93 3.1 44.5 1.0 CD A:GLU142 3.1 61.8 1.0 MN A:MN401 3.3 40.7 1.0 OE2 A:GLU93 3.3 49.3 1.0 PA A:ADV301 3.4 56.1 1.0 CD A:GLU97 3.5 40.6 1.0 OE1 A:GLU142 3.6 61.1 1.0 O A:HOH406 3.7 41.2 1.0 CG A:GLU97 3.7 39.5 1.0 MN A:MN403 3.8 61.7 1.0 O1A A:ADV301 3.8 56.9 1.0 O A:ALA76 3.9 33.9 1.0 O5' A:ADV301 4.0 57.9 1.0 C5' A:ADV301 4.2 61.9 1.0 CG A:GLU142 4.3 62.8 1.0 OE1 A:GLU96 4.4 38.1 1.0 CG A:GLU93 4.5 42.8 1.0 CX A:ADV301 4.6 51.3 1.0 OE1 A:GLU97 4.7 41.3 1.0 CA A:GLY77 4.8 31.1 1.0 O A:HOH412 4.8 41.6 1.0 CB A:GLU93 4.9 39.4 1.0 C A:ALA76 4.9 30.8 1.0

Manganese binding site 3 out of 3 in the Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of the Mt-Adprase in Complex with Three MN2+ Ions and Ampcpr, A Nudix Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn403 b:61.7 occ:1.00 O1A A:ADV301 2.1 56.9 1.0 O A:HOH404 2.1 60.3 1.0 O A:HOH405 2.1 55.3 1.0 OE2 A:GLU93 2.1 49.3 1.0 O A:HOH407 2.2 59.2 1.0 PA A:ADV301 3.3 56.1 1.0 CD A:GLU93 3.3 44.5 1.0 NH2 A:ARG92 3.4 54.0 1.0 O5' A:ADV301 3.5 57.9 1.0 MN A:MN402 3.8 55.3 1.0 O2A A:ADV301 3.8 53.9 1.0 OE1 A:GLU93 3.8 48.0 1.0 O A:HOH451 3.9 48.9 1.0 OD2 A:ASP80 4.0 44.1 1.0 N A:LEU78 4.3 33.4 1.0 CA A:GLY77 4.4 31.1 1.0 OD1 A:ASP80 4.4 44.0 1.0 CG A:GLU93 4.5 42.8 1.0 C5' A:ADV301 4.6 61.9 1.0 CZ A:ARG92 4.6 51.8 1.0 CG A:ASP80 4.6 42.8 1.0 CX A:ADV301 4.7 51.3 1.0 O A:LEU78 4.7 33.6 1.0 C A:GLY77 4.8 32.8 1.0 OE2 A:GLU142 4.8 60.1 1.0

L.-W.Kang, S.B.Gabelli, J.E.Cunningham, S.F.O'handley, L.M.Amzel. Structure and Mechanism of Mt-Adprase, A Nudix Hydrolase From Mycobacterium Tuberculosis Structure V. 11 1015 2003.
ISSN: ISSN 0969-2126
PubMed: 12906832
DOI: 10.1016/S0969-2126(03)00154-0