Iron in PDB 2ht9: The Structure of Dimeric Human Glutaredoxin 2

The structure of The Structure of Dimeric Human Glutaredoxin 2, PDB code: 2ht9 was solved by C.Johansson, C.Smee, K.L.Kavanagh, J.Debreczeni, F.Von Delft, O.Gileadi, C.Arrowsmith, J.Weigelt, A.Edwards, M.Sundstrom, U.Oppermann, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	96.67 / 1.90
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	111.754, 111.754, 51.647, 90.00, 90.00, 120.00
R / Rfree (%)	14.9 / 17.8

The binding sites of Iron atom in the The Structure of Dimeric Human Glutaredoxin 2 (pdb code 2ht9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Structure of Dimeric Human Glutaredoxin 2, PDB code: 2ht9:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The Structure of Dimeric Human Glutaredoxin 2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Dimeric Human Glutaredoxin 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:25.3 occ:1.00 FE1 A:FES1001 0.0 25.3 1.0 S1 A:FES1001 2.2 24.6 1.0 S2 A:FES1001 2.2 28.4 1.0 SG2 A:GSH200 2.3 26.8 1.0 SG A:CYS37 2.3 25.7 1.0 FE2 A:FES1001 2.8 25.4 1.0 CB2 A:GSH200 3.2 25.2 1.0 CB A:CYS37 3.3 25.9 1.0 CA A:CYS37 3.8 28.0 1.0 N A:SER38 4.0 25.9 1.0 N A:TYR39 4.1 22.7 1.0 N B:SER38 4.1 26.0 1.0 CB A:TYR39 4.1 25.3 1.0 C A:CYS37 4.1 29.1 1.0 SG2 B:GSH1200 4.4 26.2 1.0 CA B:CYS37 4.5 27.2 1.0 CA2 A:GSH200 4.6 27.6 1.0 CG A:TYR39 4.7 27.6 1.0 SG B:CYS37 4.7 26.8 1.0 CA A:TYR39 4.7 25.7 1.0 CB B:SER38 4.7 25.4 1.0 C B:CYS37 4.8 27.4 1.0 O B:SER36 4.9 31.2 1.0 CA B:SER38 4.9 24.9 1.0 CA A:SER38 5.0 24.7 1.0

Iron binding site 2 out of 2 in the The Structure of Dimeric Human Glutaredoxin 2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of Dimeric Human Glutaredoxin 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:25.4 occ:1.00 FE2 A:FES1001 0.0 25.4 1.0 S2 A:FES1001 2.2 28.4 1.0 S1 A:FES1001 2.2 24.6 1.0 SG2 B:GSH1200 2.3 26.2 1.0 SG B:CYS37 2.3 26.8 1.0 FE1 A:FES1001 2.8 25.3 1.0 CB2 B:GSH1200 3.2 24.6 1.0 CB B:CYS37 3.4 25.3 1.0 CA B:CYS37 3.7 27.2 1.0 N B:SER38 3.9 26.0 1.0 N B:TYR39 3.9 22.4 1.0 C B:CYS37 4.1 27.4 1.0 N A:SER38 4.1 25.9 1.0 CB B:TYR39 4.2 29.6 1.0 SG2 A:GSH200 4.4 26.8 1.0 CA A:CYS37 4.5 28.0 1.0 CA2 B:GSH1200 4.6 18.8 1.0 SG A:CYS37 4.7 25.7 1.0 CA B:TYR39 4.7 28.1 1.0 CG B:TYR39 4.8 26.9 1.0 C A:CYS37 4.9 29.1 1.0 CB A:SER38 4.9 29.8 1.0 CA B:SER38 4.9 24.9 1.0 C B:SER38 4.9 27.3 1.0 O A:SER36 4.9 29.6 1.0 CB A:CYS37 5.0 25.9 1.0

C.Johansson, K.L.Kavanagh, O.Gileadi, U.Oppermann. Reversible Sequestration of Active Site Cysteines in A 2FE-2S-Bridged Dimer Provides A Mechanism For Glutaredoxin 2 Regulation in Human Mitochondria J.Biol.Chem. V. 282 3077 2007.
ISSN: ISSN 0021-9258
PubMed: 17121859
DOI: 10.1074/JBC.M608179200