Manganese in PDB 3d2o: Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib

All present enzymatic activity of Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib:
3.5.4.16;

The structure of Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib, PDB code: 3d2o was solved by M.A.Swairjo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.33 / 2.04
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	92.225, 100.420, 113.947, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 26.4

The structure of Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib (pdb code 3d2o). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib, PDB code: 3d2o:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib


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 Manganese-Metallated Gtp Cyclohydrolase Type Ib within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn258 b:49.6 occ:1.00 NE2 A:HIS159 2.3 39.7 1.0 SG A:CYS147 2.4 51.3 1.0 CD2 A:HIS159 3.0 42.9 1.0 CB A:CYS147 3.3 52.5 1.0 CE1 A:HIS159 3.5 42.4 1.0 OE1 A:GLU243 4.0 56.9 1.0 CD1 A:ILE245 4.3 45.2 1.0 CG A:HIS159 4.3 46.0 1.0 ND1 A:HIS159 4.5 43.2 1.0 CB A:SER150 4.5 57.6 1.0 N A:SER150 4.5 57.1 1.0 CA A:CYS147 4.8 52.5 1.0 CB A:CYS149 4.8 57.6 1.0 CA A:SER150 5.0 57.4 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Manganese-Metallated Gtp Cyclohydrolase Type Ib


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 Manganese-Metallated Gtp Cyclohydrolase Type Ib within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn258 b:31.4 occ:1.00 NE2 B:HIS159 2.1 27.8 1.0 SG B:CYS147 2.5 34.3 1.0 N1 B:AZI261 2.7 29.5 0.5 O B:HOH406 2.7 30.0 1.0 CD2 B:HIS159 3.1 25.1 1.0 CE1 B:HIS159 3.1 27.0 1.0 CB B:CYS147 3.3 31.1 1.0 N2 B:AZI261 3.5 23.8 0.5 ND1 B:HIS159 4.2 28.8 1.0 CG B:HIS159 4.2 27.5 1.0 CB B:SER150 4.3 31.1 1.0 OE2 B:GLU243 4.4 35.2 1.0 N3 B:AZI261 4.5 33.3 0.5 N B:SER150 4.5 32.2 1.0 CD1 B:ILE245 4.5 28.8 1.0 CA B:CYS147 4.7 32.0 1.0 CB B:CYS149 4.8 34.8 1.0 CA B:SER150 4.9 31.4 1.0

B.Sankaran, S.A.Bonnett, K.Shah, S.Gabriel, R.Reddy, P.Schimmel, D.A.Rodionov, V.De Crecy-Lagard, J.D.Helmann, D.Iwata-Reuyl, M.A.Swairjo. Zinc-Independent Folate Biosynthesis: Genetic, Biochemical, and Structural Investigations Reveal New Metal Dependence For Gtp Cyclohydrolase Ib J.Bacteriol. V. 191 6936 2009.
ISSN: ISSN 0021-9193
PubMed: 19767425
DOI: 10.1128/JB.00287-09