Iron in PDB 1oii: Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate

The structure of Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate, PDB code: 1oii was solved by I.Mueller, A.Kahnert, T.Pape, T.Dierks, W.Meyer-Klauke, M.A.Kertesz, I.Uson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.19
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.421, 147.329, 158.573, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 22

The binding sites of Iron atom in the Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate (pdb code 1oii). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate, PDB code: 1oii:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate


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 the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1301 b:21.6 occ:0.70 O A:HOH2053 1.9 29.4 1.0 O5 A:AKG1302 1.9 32.4 0.7 OD2 A:ASP110 2.0 28.6 1.0 O2 A:AKG1302 2.1 26.2 0.7 NE2 A:HIS264 2.1 27.0 1.0 NE2 A:HIS108 2.2 30.6 1.0 C2 A:AKG1302 2.6 33.8 0.7 C1 A:AKG1302 2.7 32.5 0.7 CE1 A:HIS264 3.1 29.8 1.0 CG A:ASP110 3.1 29.3 1.0 CD2 A:HIS264 3.1 25.9 1.0 CE1 A:HIS108 3.1 32.8 1.0 CD2 A:HIS108 3.2 30.9 1.0 OD1 A:ASP110 3.6 31.9 1.0 O1 A:AKG1302 3.9 33.4 0.7 C3 A:AKG1302 4.1 35.0 0.7 ND1 A:HIS264 4.2 25.4 1.0 O A:HOH2150 4.2 37.2 1.0 CG A:HIS264 4.2 25.2 1.0 ND1 A:HIS108 4.3 29.1 1.0 CG A:HIS108 4.3 30.3 1.0 CB A:ASP110 4.4 28.7 1.0 C4 A:AKG1302 4.7 31.9 0.7 CZ2 A:TRP257 4.7 27.4 1.0 CA A:ASP110 4.8 28.6 1.0 O A:HOH2054 4.9 37.5 1.0

Iron binding site 2 out of 4 in the Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate


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 the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1301 b:21.8 occ:0.70 O B:HOH2155 1.9 29.8 1.0 OD2 B:ASP110 2.0 28.2 1.0 O5 B:AKG1302 2.0 26.6 0.7 O2 B:AKG1302 2.1 25.6 0.7 NE2 B:HIS264 2.1 27.5 1.0 NE2 B:HIS108 2.2 30.1 1.0 C2 B:AKG1302 2.7 28.6 0.7 C1 B:AKG1302 2.8 27.2 0.7 CE1 B:HIS264 3.1 29.7 1.0 CG B:ASP110 3.1 29.2 1.0 CD2 B:HIS264 3.1 25.8 1.0 CE1 B:HIS108 3.2 32.7 1.0 CD2 B:HIS108 3.2 30.2 1.0 OD1 B:ASP110 3.6 32.0 1.0 O1 B:AKG1302 4.0 27.1 0.7 C3 B:AKG1302 4.2 30.7 0.7 ND1 B:HIS264 4.2 25.1 1.0 CG B:HIS264 4.3 25.0 1.0 ND1 B:HIS108 4.3 29.0 1.0 CG B:HIS108 4.3 30.2 1.0 CB B:ASP110 4.5 28.8 1.0 C4 B:AKG1302 4.7 28.1 0.7 CZ2 B:TRP257 4.7 27.2 1.0 CA B:ASP110 4.9 28.6 1.0 O B:HOH2055 4.9 35.5 1.0

Iron binding site 3 out of 4 in the Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1300 b:22.3 occ:0.70 O5 C:AKG1301 1.9 27.6 0.7 O C:HOH2149 1.9 30.9 1.0 OD2 C:ASP110 2.0 28.6 1.0 O2 C:AKG1301 2.1 26.4 0.7 NE2 C:HIS264 2.1 27.9 1.0 NE2 C:HIS108 2.2 30.7 1.0 C2 C:AKG1301 2.7 30.8 0.7 C1 C:AKG1301 2.8 30.3 0.7 CE1 C:HIS264 3.1 30.2 1.0 CD2 C:HIS264 3.1 25.8 1.0 CE1 C:HIS108 3.1 32.5 1.0 CG C:ASP110 3.2 29.5 1.0 CD2 C:HIS108 3.3 30.3 1.0 OD1 C:ASP110 3.5 32.3 1.0 O1 C:AKG1301 4.0 33.3 0.7 C3 C:AKG1301 4.1 25.2 0.7 ND1 C:HIS264 4.2 24.6 1.0 CG C:HIS264 4.2 24.4 1.0 ND1 C:HIS108 4.3 28.8 1.0 CG C:HIS108 4.4 30.6 1.0 CB C:ASP110 4.5 28.6 1.0 CZ2 C:TRP257 4.6 27.6 1.0 C4 C:AKG1301 4.7 25.8 0.7 CA C:ASP110 4.8 28.7 1.0 O C:HOH2049 4.9 39.9 1.0

Iron binding site 4 out of 4 in the Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the Alkylsulfatase Atsk, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Iron and Alphaketoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1300 b:22.9 occ:0.70 O2 D:AKG1301 2.0 28.8 0.7 O5 D:AKG1301 2.0 24.9 0.7 OD2 D:ASP110 2.1 29.3 1.0 O D:HOH2115 2.1 31.7 1.0 NE2 D:HIS264 2.1 28.2 1.0 NE2 D:HIS108 2.2 30.9 1.0 C2 D:AKG1301 2.7 32.8 0.7 C1 D:AKG1301 2.7 30.0 0.7 CE1 D:HIS264 3.1 29.8 1.0 CE1 D:HIS108 3.1 32.7 1.0 CD2 D:HIS264 3.1 26.2 1.0 CG D:ASP110 3.2 29.3 1.0 CD2 D:HIS108 3.2 30.3 1.0 OD1 D:ASP110 3.6 31.9 1.0 O1 D:AKG1301 3.9 29.6 0.7 O D:HOH2116 4.0 40.0 1.0 ND1 D:HIS264 4.2 25.6 1.0 C3 D:AKG1301 4.2 30.6 0.7 CG D:HIS264 4.2 24.6 1.0 ND1 D:HIS108 4.2 29.1 1.0 CG D:HIS108 4.3 30.5 1.0 CB D:ASP110 4.5 29.2 1.0 CZ2 D:TRP257 4.7 27.5 1.0 C4 D:AKG1301 4.7 27.5 0.7 CA D:ASP110 4.8 29.2 1.0 O D:HOH2038 5.0 39.1 1.0

I.Mueller, A.Kahnert, T.Pape, G.M.Sheldrick, W.Meyer-Klaucke, T.Dierks, M.A.Kertesz, I.Uson. Crystal Structure of the Alkylsulfatase Atsk: Insights Into the Catalytic Mechanism of the Fe(II) Alpha-Ketoglutarate-Dependent Dioxygenase Superfamily Biochemistry V. 42 3075 2004.
ISSN: ISSN 0006-2960
PubMed: 15023059
DOI: 10.1021/BI035752V