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Manganese in PDB 4csw: Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase

Protein crystallography data

The structure of Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase, PDB code: 4csw was solved by M.A.Mcdonough, R.Sekirnik, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.206 / 2.82
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.300, 87.690, 90.610, 90.00, 113.10, 90.00
R / Rfree (%) 16.83 / 20.96

Other elements in 4csw:

The structure of Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase (pdb code 4csw). 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 Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase, PDB code: 4csw:

Manganese binding site 1 out of 1 in 4csw

Go back to Manganese Binding Sites List in 4csw
Manganese binding site 1 out of 1 in the Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1390

b:0.8
occ:1.00
NE2 B:HIS133 2.3 78.0 1.0
OD2 B:ASP135 2.3 0.1 1.0
NE2 B:HIS196 2.4 66.7 1.0
CE1 B:HIS133 3.1 77.3 1.0
CE1 B:HIS196 3.3 63.6 1.0
CD2 B:HIS133 3.4 77.3 1.0
CG B:ASP135 3.4 0.2 1.0
CD2 B:HIS196 3.4 62.6 1.0
OD1 B:ASP135 3.9 97.7 1.0
ND1 B:HIS133 4.2 75.7 1.0
CG B:HIS133 4.4 77.4 1.0
ND1 B:HIS196 4.4 63.7 1.0
CG B:HIS196 4.5 60.4 1.0
CB B:ASP135 4.6 86.2 1.0

Reference:

R.Chowdhury, R.Sekirnik, N.C.Brissett, T.Krojer, C.-H.Ho, S.S.Ng, I.J.Clifton, W.Ge, N.J.Kershaw, G.C.Fox, J.R.C.Muniz, M.Vollmar, C.Phillips, E.S.Pilka, K.L.Kavanagh, F.Von Deflt, U.Oppermann, M.A.Mcdonough, A.J.Doherty, C.J.Schofield. Ribosomal Oxygenases Are Structurally Conserved From Prokaryotes to Humans. Nature V. 510 422 2014.
ISSN: ISSN 0028-0836
PubMed: 24814345
DOI: 10.1038/NATURE13263
Page generated: Sat Oct 5 18:55:53 2024

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