Chlorine in PDB 1imc: Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis

All present enzymatic activity of Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis:
3.1.3.25;

The structure of Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis, PDB code: 1imc was solved by R.Bone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.200, 85.200, 152.330, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / n/a

The structure of Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis also contains other interesting chemical elements:

Manganese

(Mn)

6 atoms

The binding sites of Chlorine atom in the Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis (pdb code 1imc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis, PDB code: 1imc:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl281 b:28.9 occ:1.00 MN A:MN278 2.8 24.2 1.0 MN A:MN279 2.8 35.9 1.0 MN A:MN280 2.8 31.0 1.0 OE2 A:GLU70 3.7 32.3 1.0 OE1 A:GLU70 3.9 25.5 1.0 O A:HOH286 3.9 26.4 1.0 O A:ILE92 3.9 15.7 1.0 N A:GLY94 3.9 15.1 1.0 OD2 A:ASP90 4.1 17.4 1.0 OG1 A:THR95 4.1 21.8 1.0 CD A:GLU70 4.2 33.8 1.0 CA A:ASP93 4.4 19.4 1.0 OD1 A:ASP90 4.4 28.5 1.0 OD1 A:ASP93 4.4 19.2 1.0 O A:HOH288 4.5 35.5 1.0 N A:THR95 4.5 20.0 1.0 O A:HOH293 4.5 51.7 1.0 O A:HOH285 4.6 26.1 1.0 O A:HOH287 4.6 47.0 1.0 OD1 A:ASP220 4.6 23.2 1.0 C A:ASP93 4.7 15.0 1.0 CG A:ASP90 4.7 19.4 1.0 O A:HOH289 4.7 46.3 1.0 C A:ILE92 4.9 13.5 1.0 CA A:GLY94 4.9 16.1 1.0 CB A:THR95 5.0 14.0 1.0

Chlorine binding site 2 out of 2 in the Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl281 b:28.6 occ:1.00 MN B:MN279 2.6 34.3 1.0 MN B:MN278 2.8 22.5 1.0 MN B:MN280 2.8 38.0 1.0 O B:HOH302 3.6 42.4 1.0 OE2 B:GLU70 3.7 29.1 1.0 OD2 B:ASP90 3.8 23.6 1.0 OG1 B:THR95 3.9 27.0 1.0 N B:GLY94 3.9 14.8 1.0 O B:ILE92 3.9 13.5 1.0 OD1 B:ASP93 4.0 14.2 1.0 OE1 B:GLU70 4.0 18.6 1.0 O B:HOH286 4.2 5.1 1.0 O B:HOH287 4.2 17.1 1.0 CD B:GLU70 4.2 25.7 1.0 CA B:ASP93 4.3 18.4 1.0 OD1 B:ASP90 4.4 24.3 1.0 N B:THR95 4.4 22.1 1.0 OD1 B:ASP220 4.5 24.0 1.0 CG B:ASP90 4.6 25.9 1.0 C B:ASP93 4.6 17.0 1.0 O B:HOH288 4.7 20.0 1.0 CB B:THR95 4.8 24.7 1.0 O B:HOH285 4.8 28.8 1.0 O B:HOH284 4.8 26.6 1.0 CG B:ASP93 4.9 22.9 1.0 CA B:GLY94 4.9 15.4 1.0 C B:ILE92 4.9 17.1 1.0

R.Bone, L.Frank, J.P.Springer, J.R.Atack. Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis. Biochemistry V. 33 9468 1994.
ISSN: ISSN 0006-2960
PubMed: 8068621
DOI: 10.1021/BI00198A012