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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1imc:

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

Chlorine (Cl) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 6 binding sites of Manganese where determined in the Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis, PDB code: 1imc:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 1imc

Go back to Manganese Binding Sites List in 1imc
Manganese binding site 1 out of 6 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 Manganese with other atoms in the Mn 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:Mn278

b:24.2
occ:1.00
 O A:HOH287 2.1 47.0 1.0
OE1 A:GLU70 2.1 25.5 1.0
O A:ILE92 2.1 15.7 1.0
OD1 A:ASP90 2.3 28.5 1.0
CL A:CL281 2.8 28.9 1.0
CD A:GLU70 2.9 33.8 1.0
OE2 A:GLU70 3.1 32.3 1.0
CG A:ASP90 3.2 19.4 1.0
C A:ILE92 3.3 13.5 1.0
OD2 A:ASP90 3.4 17.4 1.0
MN A:MN280 3.8 31.0 1.0
MN A:MN279 3.9 35.9 1.0
OG1 A:THR95 4.0 21.8 1.0
CA A:ASP93 4.1 19.4 1.0
N A:ASP93 4.1 17.1 1.0
OD2 A:ASP47 4.2 33.6 1.0
N A:ILE92 4.2 13.2 1.0
O A:HOH288 4.2 35.5 1.0
CG A:GLU70 4.3 18.8 1.0
OE2 A:GLU71 4.3 38.5 1.0
CA A:ILE92 4.4 10.3 1.0
CD A:PRO91 4.6 12.9 1.0
CB A:ASP90 4.6 5.2 1.0
CB A:GLU70 4.7 23.1 1.0
N A:GLY94 4.8 15.1 1.0
CG A:PRO91 4.8 9.2 1.0
N A:PRO91 4.8 7.5 1.0
CB A:ILE92 4.9 9.8 1.0
CA A:ASP90 4.9 13.6 1.0
C A:ASP90 4.9 10.8 1.0

Manganese binding site 2 out of 6 in 1imc

Go back to Manganese Binding Sites List in 1imc
Manganese binding site 2 out of 6 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 Manganese with other atoms in the Mn 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
A:Mn279

b:35.9
occ:1.00
 OD1 A:ASP220 2.1 23.2 1.0
OD1 A:ASP93 2.3 19.2 1.0
OD2 A:ASP90 2.4 17.4 1.0
CL A:CL281 2.8 28.9 1.0
CG A:ASP220 3.3 22.3 1.0
CG A:ASP93 3.4 21.8 1.0
CG A:ASP90 3.5 19.4 1.0
O A:HOH289 3.7 46.3 1.0
MN A:MN278 3.9 24.2 1.0
OD1 A:ASP90 4.0 28.5 1.0
CA A:ASP93 4.0 19.4 1.0
OD2 A:ASP220 4.1 30.3 1.0
CB A:ASP93 4.1 19.8 1.0
CB A:ASP220 4.3 19.9 1.0
OE1 A:GLU70 4.3 25.5 1.0
CD1 A:TRP219 4.4 19.0 1.0
CA A:ASP220 4.4 21.5 1.0
OD2 A:ASP93 4.4 26.5 1.0
N A:GLY94 4.6 15.1 1.0
C A:ASP93 4.7 15.0 1.0
CB A:ASP90 4.8 5.2 1.0
NE1 A:TRP219 4.8 26.7 1.0
O A:ILE92 4.8 15.7 1.0
N A:ASP220 4.9 21.1 1.0
CD A:GLU70 5.0 33.8 1.0
O A:HOH294 5.0 53.0 1.0

Manganese binding site 3 out of 6 in 1imc

Go back to Manganese Binding Sites List in 1imc
Manganese binding site 3 out of 6 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 Manganese with other atoms in the Mn binding site number 3 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:Mn280

b:31.0
occ:1.00
 O A:HOH286 2.1 26.4 1.0
O A:HOH288 2.1 35.5 1.0
O A:HOH285 2.1 26.1 1.0
OE2 A:GLU70 2.6 32.3 1.0
CL A:CL281 2.8 28.9 1.0
O A:LEU42 3.7 23.4 1.0
CD A:GLU70 3.7 33.8 1.0
MN A:MN278 3.8 24.2 1.0
O A:HOH293 4.0 51.7 1.0
OG1 A:THR95 4.0 21.8 1.0
OD1 A:ASP41 4.2 30.6 1.0
OE1 A:GLU70 4.3 25.5 1.0
CE A:LYS36 4.4 10.6 1.0
NZ A:LYS36 4.4 10.7 1.0
OE2 A:GLU71 4.6 38.5 1.0
O A:HOH287 4.7 47.0 1.0
CB A:THR95 4.7 14.0 1.0
C A:LEU42 4.9 24.2 1.0
CG A:GLU70 4.9 18.8 1.0

Manganese binding site 4 out of 6 in 1imc

Go back to Manganese Binding Sites List in 1imc
Manganese binding site 4 out of 6 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 Manganese with other atoms in the Mn binding site number 4 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:Mn278

b:22.5
occ:1.00
 O B:HOH288 2.0 20.0 1.0
OE1 B:GLU70 2.1 18.6 1.0
O B:ILE92 2.1 13.5 1.0
OD1 B:ASP90 2.2 24.3 1.0
CL B:CL281 2.8 28.6 1.0
CD B:GLU70 2.9 25.7 1.0
CG B:ASP90 3.1 25.9 1.0
OE2 B:GLU70 3.1 29.1 1.0
OD2 B:ASP90 3.2 23.6 1.0
C B:ILE92 3.3 17.1 1.0
MN B:MN280 3.4 38.0 1.0
OG1 B:THR95 3.6 27.0 1.0
MN B:MN279 3.8 34.3 1.0
CA B:ASP93 4.0 18.4 1.0
N B:ASP93 4.1 17.3 1.0
OD2 B:ASP47 4.1 17.7 1.0
O B:HOH285 4.2 28.8 1.0
CG B:GLU70 4.3 21.3 1.0
N B:ILE92 4.3 18.6 1.0
CA B:ILE92 4.4 20.0 1.0
OE2 B:GLU71 4.4 23.2 1.0
CB B:ASP90 4.5 21.1 1.0
O B:HOH302 4.7 42.4 1.0
CD B:PRO91 4.7 15.1 1.0
CB B:GLU70 4.7 20.7 1.0
N B:GLY94 4.8 14.8 1.0
OD1 B:ASP93 4.8 14.2 1.0
CB B:ILE92 4.9 22.2 1.0
N B:PRO91 4.9 20.7 1.0
CA B:ASP90 4.9 19.9 1.0
CB B:THR95 4.9 24.7 1.0
O B:HOH286 5.0 5.1 1.0
C B:ASP93 5.0 17.0 1.0
CB B:ASP93 5.0 17.7 1.0

Manganese binding site 5 out of 6 in 1imc

Go back to Manganese Binding Sites List in 1imc
Manganese binding site 5 out of 6 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 Manganese with other atoms in the Mn binding site number 5 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:Mn279

b:34.3
occ:1.00
 OD1 B:ASP93 2.1 14.2 1.0
OD1 B:ASP220 2.2 24.0 1.0
OD2 B:ASP90 2.2 23.6 1.0
CL B:CL281 2.6 28.6 1.0
O B:HOH302 3.0 42.4 1.0
CG B:ASP220 3.1 22.1 1.0
CG B:ASP93 3.4 22.9 1.0
CG B:ASP90 3.4 25.9 1.0
MN B:MN278 3.8 22.5 1.0
OD2 B:ASP220 3.8 26.8 1.0
O B:HOH284 3.8 26.6 1.0
OD1 B:ASP90 4.0 24.3 1.0
CA B:ASP93 4.1 18.4 1.0
CB B:ASP93 4.1 17.7 1.0
CB B:ASP220 4.1 22.5 1.0
OD2 B:ASP93 4.3 19.6 1.0
CA B:ASP220 4.4 19.9 1.0
CD1 B:TRP219 4.4 17.8 1.0
OE1 B:GLU70 4.4 18.6 1.0
CB B:ASP90 4.6 21.1 1.0
NE1 B:TRP219 4.6 15.2 1.0
N B:GLY94 4.7 14.8 1.0
O B:ILE92 4.7 13.5 1.0
C B:ASP93 4.8 17.0 1.0
CD B:GLU70 4.9 25.7 1.0
OE2 B:GLU70 5.0 29.1 1.0

Manganese binding site 6 out of 6 in 1imc

Go back to Manganese Binding Sites List in 1imc
Manganese binding site 6 out of 6 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 Manganese with other atoms in the Mn binding site number 6 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:Mn280

b:38.0
occ:1.00
 O B:HOH286 2.0 5.1 1.0
O B:HOH287 2.0 17.1 1.0
O B:HOH285 2.2 28.8 1.0
OE2 B:GLU70 2.3 29.1 1.0
CL B:CL281 2.8 28.6 1.0
MN B:MN278 3.4 22.5 1.0
CD B:GLU70 3.4 25.7 1.0
OG1 B:THR95 3.4 27.0 1.0
OE1 B:GLU70 3.9 18.6 1.0
O B:LEU42 4.0 22.8 1.0
CB B:THR95 4.2 24.7 1.0
OD1 B:ASP41 4.3 23.7 1.0
OE2 B:GLU71 4.3 23.2 1.0
O B:HOH288 4.4 20.0 1.0
CE B:LYS36 4.4 31.7 1.0
O B:HOH295 4.5 25.6 1.0
O B:HOH302 4.5 42.4 1.0
NZ B:LYS36 4.5 35.0 1.0
CG B:GLU70 4.7 21.3 1.0
OD2 B:ASP47 4.9 17.7 1.0

Reference:

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
Page generated: Sat Oct 5 11:01:11 2024

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