Manganese in PDB 5vxg: Crystal Structure of Xanthomonas Campestris Olea E117Q Bound with Cerulenin

Protein crystallography data

The structure of Crystal Structure of Xanthomonas Campestris Olea E117Q Bound with Cerulenin, PDB code: 5vxg was solved by M.R.Jensen, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.55 / 2.07
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.262, 90.262, 69.416, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 24.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Xanthomonas Campestris Olea E117Q Bound with Cerulenin (pdb code 5vxg). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Xanthomonas Campestris Olea E117Q Bound with Cerulenin, PDB code: 5vxg:

Manganese binding site 1 out of 1 in 5vxg

Go back to Manganese Binding Sites List in 5vxg
Manganese binding site 1 out of 1 in the Crystal Structure of Xanthomonas Campestris Olea E117Q Bound with Cerulenin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Xanthomonas Campestris Olea E117Q Bound with Cerulenin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:40.5
occ:1.00
O A:HOH501 2.0 37.0 1.0
O A:HOH506 2.1 36.0 1.0
OD1 A:ASP76 2.3 40.8 1.0
ND1 A:HIS38 2.4 45.4 1.0
CG A:ASP76 2.9 40.7 1.0
OD2 A:ASP76 3.0 41.5 1.0
CG A:HIS38 3.3 43.9 1.0
CE1 A:HIS38 3.4 48.7 1.0
CB A:HIS38 3.5 42.4 1.0
CA A:HIS38 4.1 43.0 1.0
CB A:ASP76 4.4 38.9 1.0
CD2 A:HIS38 4.5 44.8 1.0
NE2 A:HIS38 4.5 46.6 1.0
N A:HIS38 4.8 40.7 1.0

Reference:

M.R.Jensen, B.R.Goblirsch, J.K.Christenson, M.A.Esler, F.A.Mohamed, L.P.Wackett, C.M.Wilmot. Olea GLU117 Is Key to Condensation of Two Fatty-Acyl Coenzyme A Substrates in Long-Chain Olefin Biosynthesis. Biochem. J. V. 474 3871 2017.
ISSN: ESSN 1470-8728
PubMed: 29025976
DOI: 10.1042/BCJ20170642
Page generated: Tue Dec 15 04:47:59 2020

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