Manganese in PDB 3r0i: Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid

All present enzymatic activity of Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid:
1.1.1.267;

The structure of Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid, PDB code: 3r0i was solved by C.T.Behrendt, A.Kunfermann, V.Illarionova, A.Matheeussen, M.K.Pein, T.Graewert, A.Bacher, W.Eisenreich, B.Illarionov, M.Fischer, L.Maes, M.Groll, T.Kurz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	91.254, 54.584, 107.798, 90.00, 93.17, 90.00
R / Rfree (%)	16.3 / 21.7

The structure of Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Manganese atom in the Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid (pdb code 3r0i). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid, PDB code: 3r0i:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn990 b:19.9 occ:1.00 O18 A:C0K991 2.1 30.8 1.0 O15 A:C0K991 2.1 34.8 1.0 OD1 A:ASP150 2.2 17.2 1.0 OE2 A:GLU152 2.2 14.8 1.0 OE1 A:GLU231 2.2 16.8 1.0 O A:HOH432 2.8 30.2 1.0 C14 A:C0K991 2.8 40.2 1.0 N16 A:C0K991 2.8 39.2 1.0 CG A:ASP150 3.1 22.0 1.0 CD A:GLU152 3.2 13.3 1.0 CD A:GLU231 3.3 16.9 1.0 OE1 A:GLU152 3.5 16.3 1.0 OD2 A:ASP150 3.5 20.9 1.0 OE2 A:GLU231 3.7 12.2 1.0 C17 A:C0K991 4.2 40.3 1.0 N A:SER151 4.3 11.0 1.0 C13 A:C0K991 4.4 40.0 1.0 ND2 A:ASN227 4.4 16.5 1.0 CG A:GLU231 4.4 11.6 1.0 N A:GLU152 4.4 7.1 1.0 CG A:GLU152 4.5 9.9 1.0 O A:HOH509 4.5 24.1 1.0 CB A:ASP150 4.5 13.4 1.0 CB A:SER151 4.6 9.7 1.0 NZ A:LYS125 4.6 31.1 1.0 CE A:LYS125 4.6 20.7 1.0 O A:HOH788 4.7 38.9 1.0 CB A:GLU152 4.8 7.2 1.0 OD1 A:ASN227 4.9 15.9 1.0 CA A:SER151 5.0 10.9 1.0 C A:ASP150 5.0 13.5 1.0 NZ A:LYS228 5.0 8.7 1.0

Manganese binding site 2 out of 2 in the Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Ispc in Complex with An N-Methyl-Substituted Hydroxamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn990 b:19.9 occ:1.00 OE1 B:GLU231 2.0 12.2 1.0 OD2 B:ASP150 2.0 20.9 1.0 OE2 B:GLU152 2.2 13.3 1.0 O18 B:C0K991 2.3 30.2 1.0 O15 B:C0K991 2.4 46.2 1.0 O B:HOH580 2.7 29.0 1.0 CD B:GLU231 3.0 16.4 1.0 CG B:ASP150 3.1 21.0 1.0 CD B:GLU152 3.2 12.6 1.0 C14 B:C0K991 3.3 42.5 1.0 N16 B:C0K991 3.3 39.1 1.0 OE2 B:GLU231 3.5 11.1 1.0 O B:HOH410 3.5 14.5 1.0 OE1 B:GLU152 3.6 14.6 1.0 OD1 B:ASP150 3.6 29.2 1.0 NZ B:LYS125 3.8 18.6 1.0 O B:HOH727 4.0 32.6 1.0 CG B:GLU231 4.2 10.9 1.0 ND2 B:ASN227 4.2 17.8 1.0 CB B:ASP150 4.4 14.7 1.0 N B:SER151 4.4 8.6 1.0 CG B:GLU152 4.5 9.2 1.0 N B:GLU152 4.6 8.3 1.0 O B:HOH599 4.6 29.1 1.0 C17 B:C0K991 4.7 29.7 1.0 CB B:GLU152 4.7 7.3 1.0 C13 B:C0K991 4.7 42.2 1.0 NZ B:LYS228 4.8 10.2 1.0 OD1 B:ASN227 4.9 19.3 1.0 CB B:SER151 4.9 10.7 1.0 CG B:ASN227 5.0 16.2 1.0

C.T.Behrendt, A.Kunfermann, V.Illarionova, A.Matheeussen, M.K.Pein, T.Grawert, J.Kaiser, A.Bacher, W.Eisenreich, B.Illarionov, M.Fischer, L.Maes, M.Groll, T.Kurz. Reverse Fosmidomycin Derivatives Against the Antimalarial Drug Target Ispc (Dxr). J.Med.Chem. V. 54 6796 2011.
ISSN: ISSN 0022-2623
PubMed: 21866890
DOI: 10.1021/JM200694Q