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Manganese in PDB 1imd: 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: 1imd 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 (°) 85.850, 85.850, 153.600, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / n/a

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 1imd). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structural Studies of Metal Binding By Inositol Monophosphatase: Evidence For Two-Metal Ion Catalysis, PDB code: 1imd:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1imd

Go back to Manganese Binding Sites List in 1imd
Manganese binding site 1 out of 4 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:28.3
occ:1.00
 O A:HOH281 2.0 51.5 1.0
O A:ILE92 2.0 15.1 1.0
OD1 A:ASP90 2.2 22.6 1.0
OE1 A:GLU70 2.3 26.6 1.0
O2 A:PO4280 2.3 38.1 1.0
O3 A:PO4280 2.6 44.1 1.0
P A:PO4280 2.9 38.2 1.0
CG A:ASP90 3.1 24.1 1.0
CD A:GLU70 3.2 33.9 1.0
C A:ILE92 3.2 16.6 1.0
OD2 A:ASP90 3.3 10.8 1.0
OE2 A:GLU70 3.4 35.4 1.0
O4 A:PO4280 3.6 34.5 1.0
N A:ASP93 3.9 22.6 1.0
OG1 A:THR95 3.9 24.9 1.0
CA A:ASP93 3.9 20.5 1.0
MN A:MN279 4.0 31.1 1.0
N A:ILE92 4.1 11.1 1.0
O1 A:PO4280 4.3 54.2 1.0
CA A:ILE92 4.3 12.0 1.0
OD2 A:ASP47 4.3 31.8 1.0
OE2 A:GLU71 4.4 42.2 1.0
CB A:ASP90 4.5 12.3 1.0
CG A:GLU70 4.6 26.8 1.0
CB A:ILE92 4.7 9.2 1.0
OD1 A:ASP93 4.8 40.9 1.0
CB A:ASP93 4.8 25.6 1.0
O A:HOH282 4.8 19.6 1.0
N A:PRO91 4.8 21.3 1.0
CD A:PRO91 4.8 22.9 1.0
CA A:ASP90 4.9 15.4 1.0
C A:ASP90 4.9 18.6 1.0
N A:GLY94 4.9 15.3 1.0
CB A:GLU70 5.0 32.0 1.0
CG A:PRO91 5.0 21.8 1.0

Manganese binding site 2 out of 4 in 1imd

Go back to Manganese Binding Sites List in 1imd
Manganese binding site 2 out of 4 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:31.1
occ:1.00
 O2 A:PO4280 2.1 38.1 1.0
OD1 A:ASP220 2.2 25.6 1.0
OD1 A:ASP93 2.3 40.9 1.0
OD2 A:ASP90 2.4 10.8 1.0
P A:PO4280 3.3 38.2 1.0
CG A:ASP220 3.4 25.2 1.0
CG A:ASP93 3.4 34.0 1.0
O1 A:PO4280 3.4 54.2 1.0
CG A:ASP90 3.6 24.1 1.0
O A:HOH283 3.7 35.4 1.0
MN A:MN278 4.0 28.3 1.0
OD2 A:ASP220 4.1 25.1 1.0
CB A:ASP93 4.1 25.6 1.0
O4 A:PO4280 4.1 34.5 1.0
OD1 A:ASP90 4.2 22.6 1.0
CD1 A:TRP219 4.2 32.5 1.0
CA A:ASP93 4.3 20.5 1.0
OD2 A:ASP93 4.4 38.5 1.0
O3 A:PO4280 4.4 44.1 1.0
CB A:ASP220 4.4 21.3 1.0
NE1 A:TRP219 4.5 35.7 1.0
CA A:ASP220 4.6 17.9 1.0
OE1 A:GLU70 4.6 26.6 1.0
CB A:ASP90 4.8 12.3 1.0
CD A:GLU70 4.9 33.9 1.0
OE2 A:GLU70 4.9 35.4 1.0
O A:HOH298 4.9 51.7 1.0
N A:ASP220 5.0 21.1 1.0

Manganese binding site 3 out of 4 in 1imd

Go back to Manganese Binding Sites List in 1imd
Manganese binding site 3 out of 4 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
B:Mn278

b:29.4
occ:1.00
 O B:HOH281 2.0 39.9 1.0
OE1 B:GLU70 2.1 5.7 1.0
O B:ILE92 2.1 21.7 1.0
OD1 B:ASP90 2.2 28.9 1.0
O2 B:PO4280 2.3 40.1 1.0
O3 B:PO4280 2.4 39.7 1.0
P B:PO4280 2.9 44.7 1.0
CD B:GLU70 3.0 21.5 1.0
CG B:ASP90 3.2 32.3 1.0
OE2 B:GLU70 3.2 24.2 1.0
C B:ILE92 3.3 18.5 1.0
OD2 B:ASP90 3.4 26.9 1.0
OG1 B:THR95 3.8 24.9 1.0
O4 B:PO4280 3.8 38.4 1.0
MN B:MN279 4.0 35.4 1.0
O1 B:PO4280 4.1 49.7 1.0
N B:ILE92 4.1 15.7 1.0
N B:ASP93 4.1 15.1 1.0
OD2 B:ASP47 4.1 21.9 1.0
CA B:ASP93 4.2 17.4 1.0
CA B:ILE92 4.2 20.6 1.0
CG B:GLU70 4.3 7.6 1.0
CD B:PRO91 4.3 19.6 1.0
O B:HOH283 4.5 29.2 1.0
CB B:ASP90 4.5 23.0 1.0
OE2 B:GLU71 4.6 30.2 1.0
N B:PRO91 4.6 22.4 1.0
CG B:PRO91 4.7 12.4 1.0
CB B:GLU70 4.7 23.0 1.0
CB B:ILE92 4.8 20.5 1.0
O B:HOH282 4.8 12.4 1.0
OD1 B:ASP93 4.8 36.9 1.0
CA B:ASP90 4.8 22.5 1.0
C B:ASP90 4.8 19.7 1.0

Manganese binding site 4 out of 4 in 1imd

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Manganese binding site 4 out of 4 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:Mn279

b:35.4
occ:1.00
 OD1 B:ASP220 2.2 41.4 1.0
O2 B:PO4280 2.2 40.1 1.0
OD1 B:ASP93 2.3 36.9 1.0
OD2 B:ASP90 2.4 26.9 1.0
CG B:ASP220 3.2 33.5 1.0
O1 B:PO4280 3.3 49.7 1.0
P B:PO4280 3.3 44.7 1.0
O B:HOH284 3.5 40.5 1.0
CG B:ASP90 3.5 32.3 1.0
CG B:ASP93 3.5 27.3 1.0
OD2 B:ASP220 3.8 33.4 1.0
MN B:MN278 4.0 29.4 1.0
OD1 B:ASP90 4.0 28.9 1.0
OE1 B:GLU70 4.1 5.7 1.0
O4 B:PO4280 4.2 38.4 1.0
CD1 B:TRP219 4.2 24.8 1.0
CB B:ASP220 4.2 32.6 1.0
NE1 B:TRP219 4.4 22.4 1.0
CB B:ASP93 4.4 21.6 1.0
CA B:ASP93 4.4 17.4 1.0
OD2 B:ASP93 4.4 28.8 1.0
O3 B:PO4280 4.4 39.7 1.0
OE2 B:GLU70 4.5 24.2 1.0
CA B:ASP220 4.6 31.4 1.0
CD B:GLU70 4.6 21.5 1.0
CB B:ASP90 4.8 23.0 1.0
O B:ILE92 4.8 21.7 1.0
N B:ASP220 5.0 30.6 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 11:01:38 2024

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