Iron in PDB 3ovp: Crystal Structure of Hrpe

All present enzymatic activity of Crystal Structure of Hrpe:
5.1.3.1;

The structure of Crystal Structure of Hrpe, PDB code: 3ovp was solved by W.G.Liang, S.Y.Ouyang, N.Shaw, A.Joachimiak, R.G.Zhang, Z.J.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.66 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.773, 46.758, 73.314, 90.00, 89.97, 90.00
R / Rfree (%)	14.7 / 17.4

The binding sites of Iron atom in the Crystal Structure of Hrpe (pdb code 3ovp). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Hrpe, PDB code: 3ovp:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Hrpe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Hrpe within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe229 b:9.1 occ:1.00 OD2 A:ASP175 2.1 8.9 1.0 OD1 A:ASP37 2.1 8.5 1.0 NE2 A:HIS35 2.2 5.9 1.0 ND1 A:HIS70 2.2 5.8 1.0 O A:HOH266 2.2 13.9 1.0 O A:HOH258 2.3 12.2 1.0 CD2 A:HIS35 3.1 8.4 1.0 CE1 A:HIS70 3.1 6.9 1.0 CG A:ASP37 3.1 12.1 1.0 CG A:ASP175 3.1 13.1 1.0 CE1 A:HIS35 3.2 7.9 1.0 CG A:HIS70 3.3 6.3 1.0 OD2 A:ASP37 3.5 14.9 1.0 OD1 A:ASP175 3.5 11.2 1.0 CB A:HIS70 3.7 6.7 1.0 CE A:MET72 4.2 9.7 1.0 CG A:HIS35 4.3 5.8 1.0 NE2 A:HIS70 4.3 5.9 1.0 ND1 A:HIS35 4.3 7.7 1.0 CB A:ASP175 4.4 8.4 1.0 O A:HOH319 4.4 31.1 1.0 CD2 A:HIS70 4.4 7.1 1.0 CB A:ASP37 4.4 7.4 1.0 O A:HOH254 4.7 45.2 1.0 SD A:MET72 4.9 9.4 1.0 CA A:ASP37 4.9 6.7 1.0 CG1 A:VAL195 5.0 9.8 1.0 CE A:MET141 5.0 12.2 0.5

Iron binding site 2 out of 2 in the Crystal Structure of Hrpe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Hrpe within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe229 b:8.5 occ:1.00 OD1 B:ASP37 2.1 7.1 1.0 OD2 B:ASP175 2.1 9.5 1.0 NE2 B:HIS35 2.2 6.5 1.0 ND1 B:HIS70 2.2 5.9 1.0 O B:HOH256 2.3 13.3 1.0 O B:HOH261 2.3 12.4 1.0 CG B:ASP37 3.1 11.8 1.0 CD2 B:HIS35 3.1 7.4 1.0 CE1 B:HIS70 3.1 6.7 1.0 CG B:ASP175 3.1 14.3 1.0 CE1 B:HIS35 3.3 7.9 1.0 CG B:HIS70 3.3 7.0 1.0 OD2 B:ASP37 3.5 11.8 1.0 OD1 B:ASP175 3.5 14.8 1.0 CB B:HIS70 3.7 6.8 1.0 CE B:MET72 4.2 9.6 1.0 O B:HOH279 4.2 46.8 1.0 NE2 B:HIS70 4.3 6.6 1.0 CG B:HIS35 4.3 6.2 1.0 O B:HOH372 4.3 34.2 1.0 ND1 B:HIS35 4.3 9.9 1.0 CB B:ASP37 4.4 6.8 1.0 CD2 B:HIS70 4.4 6.8 1.0 CB B:ASP175 4.4 9.2 1.0 O B:HOH356 4.7 32.2 1.0 CA B:ASP37 4.9 6.6 1.0 SD B:MET72 4.9 10.5 1.0

W.G.Liang, S.Y.Ouyang, N.Shaw, A.Joachimiak, R.G.Zhang, Z.J.Liu. Conversion of D-Ribulose 5-Phosphate to D-Xylulose 5-Phosphate: New Insights From Structural and Biochemical Studies on Human Rpe Faseb J. V. 25 497 2011.
ISSN: ISSN 0892-6638
PubMed: 20923965
DOI: 10.1096/FJ.10-171207