Iron in PDB 6bdj: Crystal Structure of Dioxygenase TETUR07G02040

The structure of Crystal Structure of Dioxygenase TETUR07G02040, PDB code: 6bdj was solved by L.Daneshian, C.R.Schlachter, M.Chruszcz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.15
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.091, 45.415, 83.040, 90.00, 94.29, 90.00
R / Rfree (%)	21.4 / 24.8

The binding sites of Iron atom in the Crystal Structure of Dioxygenase TETUR07G02040 (pdb code 6bdj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Dioxygenase TETUR07G02040, PDB code: 6bdj:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Dioxygenase TETUR07G02040


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 Dioxygenase TETUR07G02040 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:69.1 occ:1.00 OH A:TYR118 1.9 57.7 1.0 OH A:TYR163 2.2 68.1 0.5 O A:HOH401 2.2 52.3 1.0 NE2 A:HIS171 2.3 49.6 1.0 NE2 A:HIS169 2.5 55.1 1.0 CZ A:TYR118 3.0 52.8 1.0 CZ A:TYR163 3.0 68.9 0.5 CE1 A:TYR163 3.2 70.9 0.5 CD2 A:HIS171 3.2 44.5 1.0 CE1 A:HIS169 3.3 55.3 1.0 CE1 A:HIS171 3.4 47.4 1.0 O A:HOH402 3.5 57.1 1.0 CD2 A:HIS169 3.5 54.9 1.0 CE2 A:TYR118 3.6 53.7 1.0 CE1 A:TYR118 3.9 51.5 1.0 CE2 A:TYR163 4.2 74.7 0.5 O A:HOH420 4.4 45.4 1.0 CG A:HIS171 4.4 45.7 1.0 ND1 A:HIS171 4.5 46.4 1.0 ND1 A:HIS169 4.5 57.1 1.0 NH2 A:ARG166 4.5 79.7 1.0 CD1 A:TYR163 4.5 77.9 0.5 CG A:HIS169 4.6 56.1 1.0 CD2 A:TYR67 4.9 52.0 1.0 CD2 A:TYR118 4.9 50.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Dioxygenase TETUR07G02040


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 Dioxygenase TETUR07G02040 within 5.0Å range: probe atom residue distance (Å) B Occ U:Fe301 b:66.6 occ:1.00 OH U:TYR118 2.0 62.9 1.0 NE2 U:HIS169 2.1 47.5 1.0 NE2 U:HIS171 2.1 45.8 1.0 OH U:TYR163 2.3 55.3 0.5 O U:HOH403 2.4 67.3 1.0 CD2 U:HIS171 3.0 42.3 1.0 CD2 U:HIS169 3.1 45.9 1.0 CE1 U:HIS171 3.1 47.2 1.0 CE1 U:HIS169 3.1 47.8 1.0 CZ U:TYR118 3.2 53.4 1.0 CZ U:TYR163 3.3 49.7 0.5 O U:HOH421 3.4 75.0 1.0 CE1 U:TYR163 3.6 48.3 0.5 NH1 U:ARG166 4.0 66.0 1.0 CE2 U:TYR118 4.0 51.0 1.0 CE1 U:TYR118 4.1 47.4 1.0 CG U:HIS171 4.1 45.2 1.0 ND1 U:HIS171 4.2 48.2 1.0 O U:HOH401 4.2 37.9 0.5 ND1 U:HIS169 4.2 47.9 1.0 CG U:HIS169 4.2 46.5 1.0 CE2 U:TYR163 4.4 53.7 0.5 O U:HOH432 4.5 49.2 1.0 CZ U:ARG166 4.8 65.5 1.0 CD1 U:TYR163 4.9 48.5 0.5 NE U:ARG166 5.0 66.6 1.0

C.R.Schlachter, L.Daneshian, J.Amaya, V.Klapper, N.Wybouw, T.Borowski, T.Van Leeuwen, V.Grbic, M.Grbic, T.M.Makris, M.Chruszcz. Structural and Functional Characterization of An Intradiol Ring-Cleavage Dioxygenase From the Polyphagous Spider Mite Herbivore Tetranychus Urticae Koch. Insect Biochem.Mol.Biol. V. 107 19 2019.
ISSN: ISSN 0965-1748
PubMed: 30529144
DOI: 10.1016/J.IBMB.2018.12.001