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Manganese in PDB 2fc0: Wrn Exonuclease, Mn Dgmp Complex

Protein crystallography data

The structure of Wrn Exonuclease, Mn Dgmp Complex, PDB code: 2fc0 was solved by J.J.Perry, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.90 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 81.104, 81.104, 93.560, 90.00, 90.00, 120.00
R / Rfree (%) 22.3 / 23.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Wrn Exonuclease, Mn Dgmp Complex (pdb code 2fc0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Wrn Exonuclease, Mn Dgmp Complex, PDB code: 2fc0:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2fc0

Go back to Manganese Binding Sites List in 2fc0
Manganese binding site 1 out of 2 in the Wrn Exonuclease, Mn Dgmp Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Wrn Exonuclease, Mn Dgmp Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn237

b:31.4
occ:1.00
OE2 A:GLU84 2.0 28.2 1.0
OD1 A:ASP82 2.0 29.3 1.0
OD2 A:ASP216 2.1 32.7 1.0
O A:HOH257 2.2 45.0 1.0
O A:HOH425 2.2 33.8 1.0
O A:HOH369 2.3 38.4 1.0
CG A:ASP216 3.0 29.8 1.0
CD A:GLU84 3.0 27.1 1.0
CG A:ASP82 3.1 28.4 1.0
OE1 A:GLU84 3.4 28.1 1.0
CB A:ASP216 3.5 25.8 1.0
OD2 A:ASP82 3.6 27.8 1.0
MN A:MN238 3.7 42.8 1.0
O A:HOH396 3.8 45.2 1.0
OD1 A:ASP216 4.0 31.0 1.0
O A:HOH248 4.0 48.1 1.0
O A:HOH427 4.2 36.4 1.0
NH2 A:ARG196 4.3 42.6 1.0
O A:MET83 4.3 26.7 1.0
CG A:GLU84 4.4 24.7 1.0
CB A:ASP82 4.4 27.8 1.0
NE2 A:GLN101 4.4 24.8 1.0
O A:HOH426 4.5 51.3 1.0

Manganese binding site 2 out of 2 in 2fc0

Go back to Manganese Binding Sites List in 2fc0
Manganese binding site 2 out of 2 in the Wrn Exonuclease, Mn Dgmp Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Wrn Exonuclease, Mn Dgmp Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn238

b:42.8
occ:1.00
OD2 A:ASP82 2.2 27.8 1.0
O A:HOH427 2.3 36.4 1.0
O A:HOH424 2.3 41.7 1.0
O A:HOH425 2.3 33.8 1.0
O A:HOH374 2.5 34.1 1.0
O A:HOH248 3.0 48.1 1.0
CG A:ASP82 3.2 28.4 1.0
OD1 A:ASP82 3.4 29.3 1.0
O A:HOH257 3.5 45.0 1.0
MN A:MN237 3.7 31.4 1.0
O A:MET83 3.9 26.7 1.0
O A:HOH272 4.4 37.9 1.0
OD2 A:ASP143 4.4 32.9 1.0
OD1 A:ASP143 4.4 33.1 1.0
CB A:ASP82 4.5 27.8 1.0
N A:MET83 4.5 24.8 1.0
O A:VAL138 4.6 33.9 1.0
O A:HOH260 4.8 43.1 1.0
O A:HOH308 4.8 66.3 1.0
OE2 A:GLU84 4.9 28.2 1.0
CA A:ASP82 4.9 27.1 1.0
CG A:ASP143 4.9 34.0 1.0
O A:HOH369 5.0 38.4 1.0
C A:MET83 5.0 25.7 1.0

Reference:

J.J.Perry, S.M.Yannone, L.G.Holden, C.Hitomi, A.Asaithamby, S.Han, P.K.Cooper, D.J.Chen, J.A.Tainer. Wrn Exonuclease Structure and Molecular Mechanism Imply An Editing Role in Dna End Processing. Nat.Struct.Mol.Biol. V. 13 414 2006.
ISSN: ISSN 1545-9993
PubMed: 16622405
DOI: 10.1038/NSMB1088
Page generated: Sat Oct 5 14:04:21 2024

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