Iron in PDB 1gy9: Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli

All present enzymatic activity of Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli:
1.14.11.17;

The structure of Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli, PDB code: 1gy9 was solved by J.M.Elkins, N.I.Burzlaff, M.J.Ryle, J.S.Lloyd, I.J.Clifton, J.E.Baldwin, R.P.Hausinger, P.L.Roach, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.18 / 2.50
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	116.786, 116.786, 201.937, 90.00, 90.00, 120.00
R / Rfree (%)	26.1 / 29.3

The binding sites of Iron atom in the Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli (pdb code 1gy9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli, PDB code: 1gy9:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:25.5 occ:1.00 O1 A:AKG351 1.9 23.8 1.0 OD1 A:ASP101 2.1 27.8 1.0 NE2 A:HIS255 2.1 25.9 1.0 NE2 A:HIS99 2.2 24.1 1.0 O5 A:AKG351 2.2 24.4 1.0 C1 A:AKG351 2.6 25.7 1.0 C2 A:AKG351 2.8 23.0 1.0 CG A:ASP101 3.0 26.5 1.0 CE1 A:HIS255 3.0 28.1 1.0 OD2 A:ASP101 3.0 27.4 1.0 CD2 A:HIS99 3.1 24.3 1.0 CD2 A:HIS255 3.1 28.3 1.0 CE1 A:HIS99 3.2 24.8 1.0 NH1 A:ARG270 3.7 27.1 1.0 O2 A:AKG351 3.9 30.0 1.0 ND1 A:HIS255 4.1 25.2 1.0 C2 A:TAU350 4.1 30.7 1.0 CG A:HIS255 4.2 26.2 1.0 C3 A:AKG351 4.3 24.6 1.0 ND1 A:HIS99 4.3 24.7 1.0 CG A:HIS99 4.3 23.7 1.0 CB A:ASP101 4.4 25.4 1.0 CZ2 A:TRP248 4.6 28.2 1.0 OD1 A:ASN95 4.7 31.6 1.0 CG A:ASN95 4.8 32.5 1.0 C1 A:TAU350 4.9 29.5 1.0 C4 A:AKG351 4.9 25.2 1.0 ND2 A:ASN95 4.9 33.8 1.0 CZ A:ARG270 5.0 29.6 1.0 CA A:ASP101 5.0 26.0 1.0

Iron binding site 2 out of 3 in the Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe310 b:46.7 occ:0.50 NE2 A:HIS37 2.2 43.8 1.0 OE1 A:GLU33 2.2 38.4 1.0 CE1 A:HIS37 3.0 46.0 1.0 CD2 A:HIS37 3.2 41.5 1.0 CD A:GLU33 3.4 36.0 1.0 OE2 A:GLU33 4.0 41.1 1.0 ND1 A:HIS37 4.2 42.3 1.0 CG A:HIS37 4.3 36.8 1.0 CG A:GLU33 4.5 32.3 1.0 CB A:GLU33 4.7 29.8 1.0

Iron binding site 3 out of 3 in the Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Taurine/Alpha-Ketoglutarate Dioxygenase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:27.4 occ:1.00 O1 B:AKG351 1.9 23.1 1.0 OD1 B:ASP101 2.1 27.7 1.0 NE2 B:HIS99 2.1 23.7 1.0 NE2 B:HIS255 2.1 27.1 1.0 O5 B:AKG351 2.3 24.7 1.0 C1 B:AKG351 2.7 25.1 1.0 C2 B:AKG351 2.9 23.6 1.0 CG B:ASP101 3.0 26.5 1.0 CE1 B:HIS255 3.0 28.2 1.0 CD2 B:HIS255 3.0 28.0 1.0 CD2 B:HIS99 3.1 24.4 1.0 CE1 B:HIS99 3.1 25.7 1.0 OD2 B:ASP101 3.2 27.5 1.0 NH1 B:ARG270 3.8 26.8 1.0 O2 B:AKG351 4.0 28.9 1.0 ND1 B:HIS255 4.1 26.3 1.0 CG B:HIS255 4.2 26.3 1.0 ND1 B:HIS99 4.2 25.2 1.0 C2 B:TAU350 4.2 30.3 1.0 CG B:HIS99 4.2 24.2 1.0 C3 B:AKG351 4.4 25.4 1.0 CB B:ASP101 4.5 25.1 1.0 OD1 B:ASN95 4.6 31.0 1.0 CZ2 B:TRP248 4.7 27.8 1.0 CG B:ASN95 4.7 32.7 1.0 ND2 B:ASN95 4.8 33.9 1.0 C1 B:TAU350 4.8 29.1 1.0 CA B:ASP101 4.9 25.9 1.0

J.M.Elkins, M.J.Ryle, I.J.Clifton, J.C.Dunning Hotopp, J.S.Lloyd, N.I.Burzlaff, J.E.Baldwin, R.P.Hausinger, P.L.Roach. X-Ray Crystal Structure of Escherichia Coli Taurine/Alpha-Ketoglutarate Dioxygenase Complexed to Ferrous Iron and Substrates. Biochemistry V. 41 5185 2002.
ISSN: ISSN 0006-2960
PubMed: 11955067
DOI: 10.1021/BI016014E