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Copper in PDB 2xz4: Crystal Structure of the Lfz Ectodomain of the Peptidoglycan Recognition Protein Lf

Protein crystallography data

The structure of Crystal Structure of the Lfz Ectodomain of the Peptidoglycan Recognition Protein Lf, PDB code: 2xz4 was solved by N.Basbous, F.Coste, P.Leone, R.Vincentelli, J.Royet, C.Kellenberger, A.Roussel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.747 / 1.72
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 74.802, 113.443, 37.532, 90.00, 90.00, 90.00
R / Rfree (%) 16.36 / 20.14

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Lfz Ectodomain of the Peptidoglycan Recognition Protein Lf (pdb code 2xz4). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of the Lfz Ectodomain of the Peptidoglycan Recognition Protein Lf, PDB code: 2xz4:

Copper binding site 1 out of 1 in 2xz4

Go back to Copper Binding Sites List in 2xz4
Copper binding site 1 out of 1 in the Crystal Structure of the Lfz Ectodomain of the Peptidoglycan Recognition Protein Lf


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Lfz Ectodomain of the Peptidoglycan Recognition Protein Lf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu500

b:34.1
occ:0.50
O A:ILE59 2.2 17.3 1.0
O A:HOH2004 2.4 23.3 0.5
OE1 A:GLU64 2.4 21.7 1.0
OE2 A:GLU64 3.0 22.8 1.0
CD A:GLU64 3.1 26.5 1.0
C A:ILE59 3.4 16.2 1.0
CA A:LEU60 4.2 15.2 1.0
N A:LEU60 4.3 12.7 1.0
CA A:ILE59 4.3 15.8 1.0
N A:ILE59 4.4 17.7 1.0
N A:ASP61 4.4 16.6 1.0
CG A:GLU64 4.5 19.2 1.0
CB A:ILE59 4.5 17.4 1.0
C A:LEU60 4.8 17.5 1.0
OD2 A:ASP61 4.9 40.7 1.0

Reference:

N.Basbous, F.Coste, P.Leone, R.Vincentelli, J.Royet, C.Kellenberger, A.Roussel. The Drosophila Peptidoglycan-Recognition Protein Lf Interacts with Peptidoglycan-Recognition Protein Lc to Downregulate the Imd Pathway. Embo Rep. V. 12 327 2011.
ISSN: ISSN 1469-221X
PubMed: 21372849
DOI: 10.1038/EMBOR.2011.19
Page generated: Wed Jul 31 00:17:31 2024

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