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Cobalt in PDB 3oer: Crystal Structure of Trimeric Frataxin From the Yeast Saccharomyces Cerevisiae, Complexed with Cobalt

Protein crystallography data

The structure of Crystal Structure of Trimeric Frataxin From the Yeast Saccharomyces Cerevisiae, Complexed with Cobalt, PDB code: 3oer was solved by C.A.G.Soderberg, S.Rajan, O.Gakh, C.Ta, G.Isaya, S.Al-Karadaghi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.57 / 3.20
Space group I 21 3
Cell size a, b, c (Å), α, β, γ (°) 121.200, 121.200, 121.200, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.6

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Trimeric Frataxin From the Yeast Saccharomyces Cerevisiae, Complexed with Cobalt (pdb code 3oer). 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 Trimeric Frataxin From the Yeast Saccharomyces Cerevisiae, Complexed with Cobalt, PDB code: 3oer:

Cobalt binding site 1 out of 1 in 3oer

Go back to Cobalt Binding Sites List in 3oer
Cobalt binding site 1 out of 1 in the Crystal Structure of Trimeric Frataxin From the Yeast Saccharomyces Cerevisiae, Complexed with Cobalt


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 Trimeric Frataxin From the Yeast Saccharomyces Cerevisiae, Complexed with Cobalt within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1

b:79.0
occ:0.33
O A:LEU144 4.1 76.7 1.0
CB A:ASP143 4.2 71.0 1.0
CD2 A:LEU152 4.4 79.5 1.0
O A:ASP143 4.8 71.6 1.0
O A:HOH22 4.9 48.3 1.0
CD1 A:LEU145 4.9 89.9 1.0
C A:ASP143 4.9 70.4 1.0
C A:LEU144 4.9 75.9 1.0

Reference:

C.A.Soderberg, A.V.Shkumatov, S.Rajan, O.Gakh, D.I.Svergun, G.Isaya, S.Al-Karadaghi. Oligomerization Propensity and Flexibility of Yeast Frataxin Studied By X-Ray Crystallography and Small-Angle X-Ray Scattering. J.Mol.Biol. V. 414 783 2011.
ISSN: ISSN 0022-2836
PubMed: 22051511
DOI: 10.1016/J.JMB.2011.10.034
Page generated: Sun Dec 13 10:41:43 2020

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