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Cobalt in PDB 4y5t: Structure of FTMOX1 Apo with Metal Iron

Enzymatic activity of Structure of FTMOX1 Apo with Metal Iron

All present enzymatic activity of Structure of FTMOX1 Apo with Metal Iron:
1.14.11.38;

Protein crystallography data

The structure of Structure of FTMOX1 Apo with Metal Iron, PDB code: 4y5t was solved by W.Yan, Y.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.91 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.445, 45.561, 105.409, 90.00, 99.74, 90.00
R / Rfree (%) 16.4 / 20.4

Other elements in 4y5t:

The structure of Structure of FTMOX1 Apo with Metal Iron also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of FTMOX1 Apo with Metal Iron (pdb code 4y5t). 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 Structure of FTMOX1 Apo with Metal Iron, PDB code: 4y5t:

Cobalt binding site 1 out of 1 in 4y5t

Go back to Cobalt Binding Sites List in 4y5t
Cobalt binding site 1 out of 1 in the Structure of FTMOX1 Apo with Metal Iron


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of FTMOX1 Apo with Metal Iron within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co502

b:27.6
occ:1.00
OD2 B:ASP188 2.3 36.2 1.0
OE1 B:GLU186 2.3 31.6 1.0
O B:HOH626 2.5 23.0 0.7
CD B:GLU186 3.0 33.6 1.0
CG B:ASP188 3.1 45.0 1.0
OE2 B:GLU186 3.1 44.3 1.0
OD1 B:ASP188 3.2 24.3 1.0
O B:HOH601 4.0 24.7 0.8
O B:HOH609 4.0 30.5 0.9
CG B:GLU186 4.4 35.5 1.0
CB B:ASP188 4.5 24.3 1.0
CB B:GLU186 4.6 21.7 1.0
O B:HOH740 4.7 39.7 1.0

Reference:

W.Yan, H.Song, F.Song, Y.Guo, C.H.Wu, A.Sae Her, Y.Pu, S.Wang, N.Naowarojna, A.Weitz, M.P.Hendrich, C.E.Costello, L.Zhang, P.Liu, Y.Jessie Zhang. Endoperoxide Formation By An Alpha-Ketoglutarate-Dependent Mononuclear Non-Haem Iron Enzyme. Nature V. 527 539 2015.
ISSN: ESSN 1476-4687
PubMed: 26524521
DOI: 10.1038/NATURE15519
Page generated: Tue Jul 30 17:40:33 2024

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