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Manganese in PDB 2fbv: Wrn Exonuclease, Mn Complex

Protein crystallography data

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

Resolution Low / High (Å) 19.78 / 2.40
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.971, 80.971, 93.184, 90.00, 90.00, 120.00
R / Rfree (%) 23.7 / 27.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Wrn Exonuclease, Mn Complex (pdb code 2fbv). 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 Complex, PDB code: 2fbv:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2fbv

Go back to Manganese Binding Sites List in 2fbv
Manganese binding site 1 out of 2 in the Wrn Exonuclease, Mn 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 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn237

b:57.5
occ:1.00
OD2 A:ASP82 2.3 30.9 1.0
O A:HOH421 2.4 39.6 1.0
O A:HOH417 2.5 25.3 1.0
O A:HOH419 2.5 33.5 1.0
O A:HOH420 3.1 57.9 1.0
CG A:ASP82 3.3 28.8 1.0
OD1 A:ASP82 3.7 27.3 1.0
O A:HOH342 3.7 40.3 1.0
O A:HOH418 3.7 34.2 1.0
MN A:MN238 3.8 42.2 1.0
O A:MET83 3.9 32.4 1.0
O A:HOH263 4.3 46.5 1.0
OD1 A:ASP143 4.3 33.3 1.0
N A:MET83 4.5 29.8 1.0
OD2 A:ASP143 4.5 32.2 1.0
CB A:ASP82 4.6 30.0 1.0
O A:VAL138 4.7 37.8 1.0
CG A:ASP143 4.9 34.1 1.0
OE2 A:GLU84 4.9 30.1 1.0
CA A:ASP82 4.9 29.6 1.0
C A:MET83 5.0 31.4 1.0

Manganese binding site 2 out of 2 in 2fbv

Go back to Manganese Binding Sites List in 2fbv
Manganese binding site 2 out of 2 in the Wrn Exonuclease, Mn 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 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn238

b:42.2
occ:1.00
OE2 A:GLU84 2.3 30.1 1.0
OD1 A:ASP82 2.4 27.3 1.0
OD2 A:ASP216 2.5 35.1 1.0
O A:HOH418 2.6 34.2 1.0
O A:HOH419 2.6 33.5 1.0
CD A:GLU84 3.3 29.7 1.0
CG A:ASP216 3.3 31.9 1.0
CG A:ASP82 3.3 28.8 1.0
OE1 A:GLU84 3.5 30.3 1.0
OD2 A:ASP82 3.6 30.9 1.0
NH2 A:ARG196 3.7 46.6 1.0
MN A:MN237 3.8 57.5 1.0
CB A:ASP216 3.8 29.9 1.0
O A:HOH420 4.1 57.9 1.0
O A:MET83 4.3 32.4 1.0
OD1 A:ASP216 4.3 34.1 1.0
NE2 A:GLN101 4.4 31.0 1.0
CG A:GLU84 4.7 30.4 1.0
CB A:ASP82 4.7 30.0 1.0
O A:HOH421 4.7 39.6 1.0
CZ A:ARG196 5.0 48.1 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: Tue Dec 15 04:01:39 2020

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