Manganese in PDB 4bxf: 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment

The structure of 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment, PDB code: 4bxf was solved by R.Chowdhury, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	64.83 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.340, 88.390, 167.180, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 22.1

The binding sites of Manganese atom in the 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment (pdb code 4bxf). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment, PDB code: 4bxf:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn601 b:28.9 occ:1.00 O2 A:AKG901 2.2 28.6 1.0 O5 A:AKG901 2.2 33.8 1.0 OD2 A:ASP181 2.2 27.0 1.0 O A:HOH2098 2.3 30.8 1.0 NE2 A:HIS179 2.3 29.2 1.0 NE2 A:HIS240 2.4 26.8 1.0 C2 A:AKG901 2.9 31.8 1.0 C1 A:AKG901 3.0 31.0 1.0 CE1 A:HIS179 3.2 28.7 1.0 CE1 A:HIS240 3.2 26.2 1.0 O A:HOH2110 3.2 40.3 1.0 CG A:ASP181 3.3 31.4 1.0 CD2 A:HIS179 3.4 29.2 1.0 CD2 A:HIS240 3.5 26.3 1.0 OD1 A:ASP181 3.6 31.5 1.0 O1 A:AKG901 4.2 27.3 1.0 ND1 A:HIS179 4.3 30.5 1.0 CB C:HIS39 4.4 27.1 1.0 ND1 A:HIS240 4.4 27.9 1.0 C3 A:AKG901 4.4 32.9 1.0 CG A:HIS179 4.4 28.4 1.0 CG A:HIS240 4.6 24.8 1.0 CB A:ASP181 4.6 28.6 1.0 OH A:TYR167 4.7 27.7 1.0 C4 A:AKG901 4.9 36.8 1.0 N C:HIS39 4.9 32.9 1.0

Manganese binding site 2 out of 2 in the 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of 60S Ribosomal Protein L27A Histidine Hydroxylase (MINA53 Y209C) in Complex with Mn(II), 2-Oxoglutarate (2OG) and 60S Ribosomal Protein L27A (RPL27A G37C) Peptide Fragment within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn601 b:45.0 occ:1.00 O B:HOH2037 2.2 52.1 1.0 O2 B:AKG901 2.3 48.0 1.0 O5 B:AKG901 2.3 52.1 1.0 NE2 B:HIS240 2.4 37.5 1.0 NE2 B:HIS179 2.4 53.7 1.0 OD2 B:ASP181 2.5 50.6 1.0 CE1 B:HIS179 3.0 53.5 1.0 C2 B:AKG901 3.0 51.8 1.0 C1 B:AKG901 3.0 49.7 1.0 CE1 B:HIS240 3.2 39.0 1.0 CG B:ASP181 3.4 50.9 1.0 CD2 B:HIS240 3.5 40.0 1.0 CD2 B:HIS179 3.6 54.0 1.0 OD1 B:ASP181 3.6 51.2 1.0 ND1 B:HIS179 4.2 54.0 1.0 O1 B:AKG901 4.2 48.2 1.0 ND1 B:HIS240 4.4 39.1 1.0 CG B:HIS179 4.5 54.1 1.0 C3 B:AKG901 4.5 52.7 1.0 CB D:HIS39 4.5 61.2 1.0 CG B:HIS240 4.6 40.2 1.0 CB B:ASP181 4.8 48.3 1.0 C4 B:AKG901 5.0 56.7 1.0

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