Iron in PDB 1vz4: Fe-Succinate Complex of Atsk

The structure of Fe-Succinate Complex of Atsk, PDB code: 1vz4 was solved by I.Mueller, A.C.Stueckl, I.Uson, M.Kertesz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.5
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.845, 141.000, 160.149, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 28.7

The binding sites of Iron atom in the Fe-Succinate Complex of Atsk (pdb code 1vz4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Fe-Succinate Complex of Atsk, PDB code: 1vz4:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Fe-Succinate Complex of Atsk


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Fe-Succinate Complex of Atsk within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1299 b:50.1 occ:1.00 O1 A:SIN1300 2.0 48.6 1.0 OD1 A:ASP110 2.0 45.7 1.0 NE2 A:HIS108 2.2 57.3 1.0 NE2 A:HIS264 2.2 42.7 1.0 OH A:TYR168 2.3 77.1 1.0 C1 A:SIN1300 2.7 57.6 1.0 O2 A:SIN1300 2.9 51.9 1.0 CE1 A:HIS264 3.0 45.2 1.0 CE1 A:HIS108 3.1 58.9 1.0 CD2 A:HIS108 3.2 50.5 1.0 CZ A:TYR168 3.2 76.8 1.0 CG A:ASP110 3.2 52.3 1.0 CD2 A:HIS264 3.3 36.4 1.0 OD2 A:ASP110 3.6 58.9 1.0 NH1 A:ARG279 3.9 72.2 1.0 CE1 A:TYR168 3.9 70.9 1.0 CE2 A:TYR168 3.9 75.2 1.0 C2 A:SIN1300 4.0 51.6 1.0 ND1 A:HIS108 4.2 53.7 1.0 ND1 A:HIS264 4.2 35.3 1.0 CG A:HIS108 4.3 56.4 1.0 O A:HOH2013 4.3 54.7 1.0 CG A:HIS264 4.3 37.8 1.0 CB A:ASP110 4.4 51.0 1.0 NE A:ARG279 4.5 66.9 1.0 CZ2 A:TRP257 4.6 47.6 1.0 CA A:ASP110 4.6 51.3 1.0 CZ A:ARG279 4.6 68.9 1.0 N A:ASP110 4.9 51.8 1.0 CB A:ALA104 5.0 50.4 1.0

Iron binding site 2 out of 2 in the Fe-Succinate Complex of Atsk


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Fe-Succinate Complex of Atsk within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1301 b:45.8 occ:1.00 NE2 D:HIS264 2.0 41.5 1.0 OD1 D:ASP110 2.0 39.5 1.0 O1 D:SIN1302 2.1 43.7 1.0 OH D:TYR168 2.2 45.8 1.0 NE2 D:HIS108 2.3 49.9 1.0 O2 D:SIN1302 2.5 55.2 1.0 C1 D:SIN1302 2.6 53.9 1.0 CE1 D:HIS264 2.8 30.9 1.0 CD2 D:HIS264 3.1 39.1 1.0 CD2 D:HIS108 3.1 53.4 1.0 CZ D:TYR168 3.2 49.4 1.0 CG D:ASP110 3.2 51.7 1.0 CE1 D:HIS108 3.3 49.5 1.0 NH1 D:ARG279 3.6 53.7 1.0 OD2 D:ASP110 3.7 48.9 1.0 CE2 D:TYR168 3.8 52.1 1.0 ND1 D:HIS264 3.9 36.0 1.0 O D:HOH2015 4.0 56.5 1.0 C2 D:SIN1302 4.1 51.2 1.0 CG D:HIS264 4.1 35.9 1.0 CE1 D:TYR168 4.1 42.8 1.0 CG D:HIS108 4.3 51.8 1.0 ND1 D:HIS108 4.4 47.5 1.0 CB D:ASP110 4.4 51.7 1.0 CZ2 D:TRP257 4.6 42.1 1.0 CA D:ASP110 4.6 49.6 1.0 C3 D:SIN1302 4.7 54.6 1.0 CZ D:ARG279 4.8 44.4 1.0 N D:ASP110 4.9 45.7 1.0

I.Mueller, A.C.Stueckl, J.Wakeley, M.Kertesz, I.Uson. Succinate Complex Crystal Structures of the Alpha-Ketoglutarate-Dependent Dioxygenase Atsk: Steric Aspects of Enzyme Self-Hydroxylation J.Biol.Chem. V. 280 5716 2005.
ISSN: ISSN 0021-9258
PubMed: 15542595
DOI: 10.1074/JBC.M410840200