Iron in PDB 6ojw: Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda

All present enzymatic activity of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda:
1.13.11.43;

The structure of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda, PDB code: 6ojw was solved by E.Kuatsjah, M.M.Verstraete, M.J.Kobylarz, A.K.N.Liu, M.E.P.Murphy, L.D.Eltis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.35 / 2.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	183.259, 183.259, 95.081, 90.00, 90.00, 120.00
R / Rfree (%)	18.7 / 21.5

The structure of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Iron atom in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda (pdb code 6ojw). 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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda, PDB code: 6ojw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda


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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:34.1 occ:1.00 NE2 B:HIS218 2.0 39.0 1.0 NE2 B:HIS472 2.1 35.5 1.0 NE2 B:HIS282 2.2 32.8 1.0 NE2 B:HIS167 2.3 26.1 1.0 O B:HOH752 2.5 29.4 1.0 CE1 B:HIS218 2.7 36.8 1.0 HE1 B:HIS218 2.8 44.1 1.0 CD2 B:HIS282 3.0 28.5 1.0 CD2 B:HIS472 3.0 31.6 1.0 CE1 B:HIS472 3.1 26.2 1.0 CE1 B:HIS167 3.1 30.9 1.0 CD2 B:HIS218 3.1 37.4 1.0 HD2 B:HIS282 3.1 34.2 1.0 HE1 B:HIS167 3.2 37.1 1.0 HD2 B:HIS472 3.2 38.0 1.0 CE1 B:HIS282 3.2 35.9 1.0 HE1 B:HIS472 3.3 31.4 1.0 CD2 B:HIS167 3.4 33.7 1.0 HD2 B:HIS218 3.4 44.9 1.0 HE1 B:HIS282 3.5 43.0 1.0 HD2 B:HIS167 3.6 40.5 1.0 HG23 B:THR121 3.8 41.1 1.0 HG21 B:THR121 3.9 41.1 1.0 HG22 B:THR121 3.9 41.1 1.0 ND1 B:HIS218 3.9 32.6 1.0 CG2 B:THR121 4.1 34.2 1.0 CG B:HIS218 4.1 32.2 1.0 ND1 B:HIS472 4.2 22.9 1.0 CG B:HIS472 4.2 26.8 1.0 CG B:HIS282 4.2 37.4 1.0 ND1 B:HIS167 4.3 31.5 1.0 ND1 B:HIS282 4.3 38.9 1.0 CG B:HIS167 4.4 31.6 1.0 HD22 B:LEU471 4.5 35.4 1.0 HD1 B:HIS218 4.7 39.2 1.0 HB3 B:LEU471 4.9 35.6 1.0 HD1 B:HIS472 4.9 27.5 1.0 HE1 B:PHE351 5.0 38.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda


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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:38.2 occ:1.00 NE2 A:HIS218 2.0 49.9 1.0 NE2 A:HIS472 2.1 38.5 1.0 NE2 A:HIS282 2.2 32.8 1.0 NE2 A:HIS167 2.4 34.1 1.0 O A:HOH741 2.5 34.0 1.0 CE1 A:HIS218 2.7 44.2 1.0 HE1 A:HIS218 2.8 53.0 1.0 CE1 A:HIS472 3.0 34.6 1.0 CD2 A:HIS472 3.1 31.5 1.0 CD2 A:HIS282 3.1 32.7 1.0 CE1 A:HIS282 3.1 35.9 1.0 CD2 A:HIS218 3.1 40.9 1.0 HE1 A:HIS472 3.2 41.5 1.0 HD2 A:HIS282 3.2 39.3 1.0 HD2 A:HIS472 3.3 37.8 1.0 CE1 A:HIS167 3.3 36.3 1.0 HE1 A:HIS282 3.3 43.0 1.0 HE1 A:HIS167 3.4 43.6 1.0 CD2 A:HIS167 3.4 37.4 1.0 HD2 A:HIS218 3.5 49.1 1.0 HD2 A:HIS167 3.6 44.9 1.0 HG23 A:THR121 3.9 48.3 1.0 ND1 A:HIS218 3.9 40.7 1.0 HG22 A:THR121 4.1 48.3 1.0 HG21 A:THR121 4.1 48.3 1.0 ND1 A:HIS472 4.1 30.4 1.0 CG A:HIS218 4.1 40.3 1.0 CG A:HIS472 4.2 27.9 1.0 ND1 A:HIS282 4.2 31.4 1.0 CG A:HIS282 4.2 32.9 1.0 CG2 A:THR121 4.3 40.2 1.0 ND1 A:HIS167 4.4 36.4 1.0 CG A:HIS167 4.5 35.3 1.0 HD22 A:LEU471 4.6 41.1 1.0 HD1 A:HIS218 4.7 48.9 1.0 HB3 A:LEU471 4.9 39.0 1.0 HE1 A:PHE351 4.9 39.5 1.0 HD1 A:HIS472 4.9 36.5 1.0 HD1 A:HIS282 5.0 37.7 1.0

E.Kuatsjah, M.M.Verstraete, M.J.Kobylarz, A.K.N.Liu, M.E.P.Murphy, L.D.Eltis. Identification of Functionally Important Residues and Structural Features in A Bacterial Lignostilbene Dioxygenase. J.Biol.Chem. V. 294 12911 2019.
ISSN: ESSN 1083-351X
PubMed: 31292192
DOI: 10.1074/JBC.RA119.009428