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Manganese in PDB 3m0k: Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate

Enzymatic activity of Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate

All present enzymatic activity of Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate:
3.7.1.1;

Protein crystallography data

The structure of Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate, PDB code: 3m0k was solved by O.Herzberg, C.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.92 / 1.65
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.131, 82.131, 72.717, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 20.1

Other elements in 3m0k:

The structure of Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate (pdb code 3m0k). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate, PDB code: 3m0k:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3m0k

Go back to Manganese Binding Sites List in 3m0k
Manganese binding site 1 out of 2 in the Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:16.3
occ:0.67
MN A:MN502 0.0 16.3 0.7
MN A:MN502 1.7 9.5 0.3
OD2 A:ASP155 2.2 14.7 1.0
O A:HOH601 2.2 28.6 1.0
O A:HOH661 2.3 9.8 1.0
O1 A:OXL501 2.3 11.4 0.7
O2 A:OXL501 2.4 17.7 0.7
C1 A:OXL501 3.0 14.8 0.7
C2 A:OXL501 3.1 19.0 0.7
O A:HOH786 3.1 28.6 1.0
CG A:ASP155 3.1 14.7 1.0
OD1 A:ASP155 3.6 12.7 1.0
O A:HOH660 3.7 34.8 1.0
OD1 A:ASP157 3.9 15.4 1.0
OD2 A:ASP126 3.9 15.7 1.0
O A:HOH648 3.9 27.8 1.0
CA A:GLY114 4.2 12.7 1.0
NH1 A:ARG229 4.2 15.6 1.0
N A:GLY114 4.2 12.9 1.0
N A:ALA115 4.3 14.1 1.0
CB A:ASP155 4.3 11.7 1.0
O3 A:OXL501 4.4 14.8 0.7
O4 A:OXL501 4.4 21.6 0.7
CE1 A:HIS182 4.5 15.2 1.0
OD1 A:ASP126 4.6 12.7 1.0
C A:GLY114 4.6 9.7 1.0
OH A:TYR111 4.7 13.2 1.0
CG A:ASP126 4.7 17.7 1.0
CG A:ASP157 4.8 13.0 1.0
OE1 A:GLU184 4.8 15.7 1.0

Manganese binding site 2 out of 2 in 3m0k

Go back to Manganese Binding Sites List in 3m0k
Manganese binding site 2 out of 2 in the Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Oxaloacetate Acetylhydrolase in Complex with the Product Oxalate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:9.5
occ:0.33
MN A:MN502 0.0 9.5 0.3
MN A:MN502 1.7 16.3 0.7
O A:HOH786 2.1 28.6 1.0
OD1 A:ASP157 2.2 15.4 1.0
O A:HOH661 2.3 9.8 1.0
OD2 A:ASP155 2.3 14.7 1.0
O A:HOH601 2.7 28.6 1.0
O A:HOH660 2.7 34.8 1.0
CG A:ASP155 3.2 14.7 1.0
CG A:ASP157 3.2 13.0 1.0
OD1 A:ASP155 3.4 12.7 1.0
O1 A:OXL501 3.7 11.4 0.7
OD2 A:ASP157 3.7 12.0 1.0
OD1 A:ASP126 3.9 12.7 1.0
O A:HOH659 3.9 13.4 1.0
O2 A:OXL501 4.0 17.7 0.7
OD2 A:ASP126 4.0 15.7 1.0
CA A:GLY114 4.1 12.7 1.0
CG A:ASP126 4.4 17.7 1.0
CB A:ASP157 4.4 8.9 1.0
O A:HOH667 4.4 20.9 1.0
OE1 A:GLU184 4.5 15.7 1.0
CB A:ASP155 4.6 11.7 1.0
CA A:ASP157 4.6 13.5 1.0
C1 A:OXL501 4.6 14.8 0.7
N A:ALA115 4.6 14.1 1.0
C A:GLY114 4.6 9.7 1.0
N A:GLY114 4.7 12.9 1.0
C2 A:OXL501 4.7 19.0 0.7
N A:ASP157 4.9 11.8 1.0
OE2 A:GLU184 5.0 21.7 1.0

Reference:

C.Chen, Q.Sun, B.Narayanan, D.L.Nuss, O.Herzberg. Structure of Oxalacetate Acetylhydrolase, A Virulence Factor of the Chestnut Blight Fungus. J.Biol.Chem. V. 285 26685 2010.
ISSN: ISSN 0021-9258
PubMed: 20558740
DOI: 10.1074/JBC.M110.117804
Page generated: Tue Dec 15 04:12:04 2020

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