Iron in PDB 2qh1: Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State

The structure of Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State, PDB code: 2qh1 was solved by A.U.Singer, M.Proudfoot, G.Brown, L.Xu, A.Savchenko, A.F.Yakunin, Midwestcenter For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.67 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.806, 63.031, 97.474, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 23.7

The binding sites of Iron atom in the Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State (pdb code 2qh1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State, PDB code: 2qh1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2500 b:35.1 occ:1.00 SG A:CYS149 2.0 31.0 1.0 SG A:CYS169 2.2 20.9 1.0 SG A:CYS146 2.4 25.3 1.0 CB A:CYS146 2.7 24.4 1.0 SG A:CYS174 3.0 32.6 1.0 CB A:CYS169 3.2 22.7 1.0 CB A:CYS149 3.2 31.3 1.0 CB A:CYS174 3.4 32.8 1.0 N A:CYS149 3.7 30.7 1.0 CA A:CYS149 4.0 30.6 1.0 CB A:ASN171 4.0 32.4 1.0 N A:GLY152 4.2 25.7 1.0 CA A:GLY152 4.2 24.7 1.0 CA A:CYS146 4.2 25.0 1.0 CA A:CYS169 4.6 23.6 1.0 N A:GLY150 4.6 30.0 1.0 C A:GLY152 4.6 24.7 1.0 C A:CYS149 4.6 30.8 1.0 O A:GLY152 4.7 24.7 1.0 ND2 A:ASN171 4.7 32.9 1.0 C A:CYS146 4.8 25.9 1.0 C A:LYS148 4.9 30.0 1.0 CG A:ASN171 4.9 32.6 1.0 CA A:CYS174 4.9 33.6 1.0 CB A:TYR176 4.9 30.7 1.0

Iron binding site 2 out of 2 in the Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of TA289, A Cbs-Rubredoxin-Like Protein, in Its Fe+2-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2501 b:26.7 occ:1.00 SG B:CYS174 2.2 32.4 1.0 SG B:CYS146 2.3 21.1 1.0 SG B:CYS169 2.5 26.8 1.0 SG B:CYS149 2.7 30.1 1.0 CB B:CYS174 2.9 37.1 1.0 CB B:CYS146 3.1 21.5 1.0 CB B:CYS169 3.2 26.1 1.0 CB B:CYS149 3.5 29.6 1.0 N B:CYS149 3.7 29.5 1.0 CB B:TYR176 3.9 35.5 1.0 CA B:CYS149 4.2 29.9 1.0 CB B:LYS148 4.3 29.9 1.0 CA B:CYS174 4.4 38.2 1.0 CA B:CYS146 4.6 23.0 1.0 CB B:ASN171 4.6 32.7 1.0 CA B:CYS169 4.6 26.3 1.0 C B:CYS174 4.7 39.4 1.0 C B:LYS148 4.7 29.5 1.0 O B:HOH1161 4.7 36.1 1.0 CG B:TYR176 4.7 35.2 1.0 N B:TYR176 4.8 37.9 1.0 CA B:LYS148 4.9 28.9 1.0 ND2 B:ASN171 4.9 31.1 1.0 N B:LYS148 4.9 27.2 1.0 N B:GLY152 4.9 30.8 1.0 CA B:GLY152 5.0 30.3 1.0 CA B:TYR176 5.0 35.5 1.0 O B:CYS174 5.0 38.9 1.0

M.Proudfoot, S.A.Sanders, A.Singer, R.Zhang, G.Brown, A.Binkowski, L.Xu, J.A.Lukin, A.G.Murzin, A.Joachimiak, C.H.Arrowsmith, A.M.Edwards, A.V.Savchenko, A.F.Yakunin. Biochemical and Structural Characterization of A Novel Family of Cystathionine Beta-Synthase Domain Proteins Fused to A Zn Ribbon-Like Domain. J.Mol.Biol. V. 375 301 2008.
ISSN: ISSN 0022-2836
PubMed: 18021800
DOI: 10.1016/J.JMB.2007.10.060