Manganese in PDB 3hqr: PHD2:Mn:Nog:HIF1-Alpha Substrate Complex

The structure of PHD2:Mn:Nog:HIF1-Alpha Substrate Complex, PDB code: 3hqr was solved by R.Chowdhury, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.18 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.379, 68.798, 72.221, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 24.8

The binding sites of Manganese atom in the PHD2:Mn:Nog:HIF1-Alpha Substrate Complex (pdb code 3hqr). 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 PHD2:Mn:Nog:HIF1-Alpha Substrate Complex, PDB code: 3hqr:

Manganese binding site 1 out of 1 in the PHD2:Mn:Nog:HIF1-Alpha Substrate Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of PHD2:Mn:Nog:HIF1-Alpha Substrate Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:12.8 occ:1.00 NE2 A:HIS374 1.9 12.6 1.0 OD1 A:ASP315 2.0 18.5 1.0 O2' A:OGA600 2.0 20.3 1.0 NE2 A:HIS313 2.1 8.2 1.0 O A:HOH1011 2.2 17.2 1.0 O2 A:OGA600 2.4 23.4 1.0 C2 A:OGA600 2.8 21.9 1.0 CE1 A:HIS374 2.8 9.4 1.0 CG A:ASP315 2.9 15.4 1.0 C1 A:OGA600 3.0 19.2 1.0 CE1 A:HIS313 3.0 6.2 1.0 CD2 A:HIS374 3.0 9.2 1.0 CD2 A:HIS313 3.1 7.6 1.0 OD2 A:ASP315 3.2 11.8 1.0 ND1 A:HIS374 4.0 12.0 1.0 N1 A:OGA600 4.0 21.3 1.0 CG A:HIS374 4.1 10.8 1.0 ND1 A:HIS313 4.1 10.6 1.0 O1 A:OGA600 4.2 17.4 1.0 CG S:PRO564 4.2 14.3 1.0 CG A:HIS313 4.2 8.6 1.0 O A:HOH1006 4.2 19.2 1.0 CB A:ASP315 4.2 13.4 1.0 CD S:PRO564 4.3 13.2 1.0 CA A:ASP315 4.6 13.5 1.0 CZ A:PHE366 4.6 12.2 1.0 C4 A:OGA600 4.6 17.3 1.0 N A:ASP315 4.6 10.5 1.0 CB S:PRO564 4.8 14.2 1.0 CE2 A:TYR310 4.8 16.6 1.0 CZ2 A:TRP389 4.8 14.9 1.0 CD2 A:TYR310 5.0 15.5 1.0

R.Chowdhury, M.A.Mcdonough, J.Mecinovic, C.Loenarz, E.Flashman, K.S.Hewitson, C.Domene, C.J.Schofield. Structural Basis For Binding of Hypoxia-Inducible Factor to the Oxygen-Sensing Prolyl Hydroxylases Structure V. 17 981 2009.
ISSN: ISSN 0969-2126
PubMed: 19604478
DOI: 10.1016/J.STR.2009.06.002