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Cobalt in PDB 3ozi: Crystal Structure of the Tir Domain From the Flax Disease Resistance Protein L6

Protein crystallography data

The structure of Crystal Structure of the Tir Domain From the Flax Disease Resistance Protein L6, PDB code: 3ozi was solved by T.Ve, M.Bernoux, S.Williams, E.Valkov, C.Warren, D.Hatters, J.G.Ellis, P.N.Dodds, B.Kobe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.30 / 2.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.941, 102.241, 58.300, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 23

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of the Tir Domain From the Flax Disease Resistance Protein L6 (pdb code 3ozi). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of the Tir Domain From the Flax Disease Resistance Protein L6, PDB code: 3ozi:

Cobalt binding site 1 out of 1 in 3ozi

Go back to Cobalt Binding Sites List in 3ozi
Cobalt binding site 1 out of 1 in the Crystal Structure of the Tir Domain From the Flax Disease Resistance Protein L6


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of the Tir Domain From the Flax Disease Resistance Protein L6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co205

b:29.0
occ:0.50
O A:HOH245 2.5 23.6 1.0
O A:HOH243 2.5 24.4 1.0
O A:LYS63 3.7 24.2 1.0
O A:HOH259 4.2 31.9 1.0
OE2 A:GLU37 4.3 21.1 1.0
OE1 A:GLU37 4.4 26.3 1.0
HB3 A:LYS63 4.6 32.1 1.0
HA A:ILE64 4.6 21.1 1.0
CD A:GLU37 4.7 26.2 1.0
O A:HOH234 4.8 26.0 1.0
H A:HIS65 4.8 22.7 1.0
C A:LYS63 4.8 28.9 1.0
HB2 A:HIS65 5.0 20.8 1.0

Reference:

M.Bernoux, T.Ve, S.Williams, C.Warren, D.Hatters, E.Valkov, X.Zhang, J.G.Ellis, B.Kobe, P.N.Dodds. Structural and Functional Analysis of A Plant Resistance Protein Tir Domain Reveals Interfaces For Self-Association, Signaling, and Autoregulation. Cell Host Microbe V. 9 200 2011.
ISSN: ISSN 1931-3128
PubMed: 21402359
DOI: 10.1016/J.CHOM.2011.02.009
Page generated: Sun Dec 13 10:41:51 2020

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