Manganese in PDB 4gqu: Crystal Structure of Hisb From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of Hisb From Mycobacterium Tuberculosis:
4.2.1.19;

The structure of Crystal Structure of Hisb From Mycobacterium Tuberculosis, PDB code: 4gqu was solved by M.S.Ahangar, R.Vyas, N.Nasir, B.K.Biswal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.59 / 2.02
Space group	P 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	112.539, 112.539, 112.539, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 24

The binding sites of Manganese atom in the Crystal Structure of Hisb From Mycobacterium Tuberculosis (pdb code 4gqu). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Hisb From Mycobacterium Tuberculosis, PDB code: 4gqu:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Hisb From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Hisb From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:30.5 occ:1.00 NE2 A:HIS152 2.1 30.7 1.0 NE2 A:HIS73 2.1 28.3 1.0 O A:HOH425 2.2 32.8 1.0 OE1 A:GLU77 2.3 30.5 1.0 CD2 A:HIS152 3.0 30.2 1.0 CE1 A:HIS73 3.1 28.2 1.0 CD A:GLU77 3.2 31.1 1.0 CD2 A:HIS73 3.2 28.3 1.0 CE1 A:HIS152 3.2 31.3 1.0 OE2 A:GLU77 3.6 30.8 1.0 CG A:HIS152 4.2 30.3 1.0 ND1 A:HIS73 4.2 28.4 1.0 ND1 A:HIS152 4.3 30.8 1.0 CG A:HIS73 4.3 28.6 1.0 CG A:GLU77 4.3 30.7 1.0 CB A:GLU77 4.6 30.2 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Hisb From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Hisb From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:33.1 occ:1.00 O A:HOH506 2.1 44.0 1.0 OE1 A:GLU180 2.2 34.0 1.0 NE2 A:HIS47 2.3 33.4 1.0 O A:HOH438 2.4 42.3 1.0 NE2 A:HIS176 2.4 30.4 1.0 CD A:GLU180 3.1 32.9 1.0 CD2 A:HIS47 3.1 32.5 1.0 CD2 A:HIS176 3.3 29.2 1.0 CE1 A:HIS47 3.3 33.7 1.0 CE1 A:HIS176 3.4 30.2 1.0 OE2 A:GLU180 3.4 34.3 1.0 CG A:HIS47 4.4 32.1 1.0 CG A:HIS176 4.4 29.1 1.0 ND1 A:HIS47 4.4 32.9 1.0 ND1 A:HIS176 4.5 29.9 1.0 CG A:GLU180 4.5 31.0 1.0 CE A:MET107 4.6 37.7 0.7 O A:HOH505 4.6 41.0 1.0 CE A:MET48 4.8 27.9 1.0 CB A:GLU180 4.9 29.8 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Hisb From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Hisb From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn303 b:40.5 occ:0.33 NH2 A:ARG168 3.5 32.5 1.0 NH1 A:ARG168 3.8 32.5 1.0 CZ A:ARG168 4.1 32.3 1.0 CZ A:PHE104 4.3 26.8 1.0 CE1 A:PHE104 4.7 27.2 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Hisb From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Hisb From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn304 b:90.9 occ:1.00 O1 A:EDO305 2.8 55.5 1.0 C1 A:EDO305 3.3 55.5 1.0 NH2 A:ARG151 3.6 30.9 1.0 NH1 A:ARG151 3.8 30.3 1.0 CZ A:ARG151 4.2 30.7 1.0 O A:HOH498 4.4 46.6 1.0 C2 A:EDO305 4.6 55.8 1.0

M.S.Ahangar, R.Vyas, N.Nasir, B.K.Biswal. Crystal Structures of the Native, Substrate- Bound and Inhibited Forms of Mycobacterium Tuberculosis Imidazole Glycerol Phosphate Dehydratase Acta Crystallogr.,Sect.D 2013.
ISSN: ISSN 0907-4449