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Lead in PDB 2qkl: The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex

Enzymatic activity of The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex

All present enzymatic activity of The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex:
3.6.1.30;

Protein crystallography data

The structure of The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex, PDB code: 2qkl was solved by M.She, N.Chen, H.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.33
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.723, 49.665, 115.052, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 25.9

Lead Binding Sites:

The binding sites of Lead atom in the The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex (pdb code 2qkl). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total only one binding site of Lead was determined in the The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex, PDB code: 2qkl:

Lead binding site 1 out of 1 in 2qkl

Go back to Lead Binding Sites List in 2qkl
Lead binding site 1 out of 1 in the The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of The Crystal Structure of Fission Yeast Mrna Decapping Enzyme DCP1-DCP2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pb96

b:62.3
occ:1.00
O B:GLU32 4.4 47.9 1.0
CB B:GLU32 4.4 47.9 1.0
CG B:GLU32 4.6 49.1 1.0
CB B:PHE36 4.6 46.1 1.0
C B:GLU32 4.7 47.6 1.0
CD B:GLU32 5.0 50.7 1.0

Reference:

M.She, C.J.Decker, D.I.Svergun, A.Round, N.Chen, D.Muhlrad, R.Parker, H.Song. Structural Basis of DCP2 Recognition and Activation By DCP1. Mol.Cell V. 29 337 2008.
ISSN: ISSN 1097-2765
PubMed: 18280239
DOI: 10.1016/J.MOLCEL.2008.01.002
Page generated: Wed Dec 16 02:02:06 2020

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