Iron in PDB 4ysk: Crystal Structure of Apo-Form Sdoa From Pseudomonas Putida

The structure of Crystal Structure of Apo-Form Sdoa From Pseudomonas Putida, PDB code: 4ysk was solved by S.A.Sattler, X.Wang, P.J.Dehan, L.Xun, C.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.63 / 2.47
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	79.505, 79.505, 94.523, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 26.2

The binding sites of Iron atom in the Crystal Structure of Apo-Form Sdoa From Pseudomonas Putida (pdb code 4ysk). 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 Apo-Form Sdoa From Pseudomonas Putida, PDB code: 4ysk:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Apo-Form Sdoa From Pseudomonas Putida


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 Apo-Form Sdoa From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:36.3 occ:1.00 OD2 A:ASP170 2.0 36.7 1.0 O A:HOH419 2.1 35.1 1.0 O A:HOH452 2.2 32.0 1.0 NE2 A:HIS74 2.4 31.1 1.0 NE2 A:HIS149 2.5 31.5 1.0 O A:HOH454 3.0 34.9 1.0 CG A:ASP170 3.1 34.6 1.0 CE1 A:HIS74 3.1 32.1 1.0 CD2 A:HIS149 3.2 24.9 1.0 CD2 A:HIS74 3.5 35.6 1.0 CE1 A:HIS149 3.6 35.0 1.0 CB A:ASP170 3.7 33.7 1.0 OD1 A:ASP78 3.8 48.5 1.0 OD1 A:ASP170 4.1 31.2 1.0 ND1 A:HIS74 4.4 38.1 1.0 CG A:HIS149 4.4 25.3 1.0 ND1 A:HIS149 4.6 31.0 1.0 CG A:HIS74 4.6 33.3 1.0 ND1 A:HIS76 4.7 34.4 1.0 CE1 A:HIS212 4.7 39.6 1.0 N A:ALA77 4.7 31.4 1.0 CA A:HIS76 4.7 31.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Apo-Form Sdoa From Pseudomonas Putida


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 Apo-Form Sdoa From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:40.2 occ:1.00 OD2 B:ASP170 2.0 39.2 1.0 O B:HOH411 2.3 31.7 1.0 NE2 B:HIS74 2.4 28.8 1.0 NE2 B:HIS149 2.6 32.2 1.0 O B:HOH446 2.6 28.2 1.0 CG B:ASP170 3.1 39.1 1.0 CD2 B:HIS149 3.2 25.8 1.0 CE1 B:HIS74 3.3 32.7 1.0 CD2 B:HIS74 3.5 30.9 1.0 OD1 B:ASP78 3.6 43.2 1.0 CE1 B:HIS149 3.7 32.5 1.0 CB B:ASP170 3.7 34.1 1.0 O B:HOH433 4.1 38.6 1.0 OD1 B:ASP170 4.2 36.5 1.0 ND1 B:HIS74 4.5 37.6 1.0 CG B:HIS149 4.5 31.6 1.0 CE1 B:HIS212 4.5 42.2 1.0 N B:ALA77 4.5 33.1 1.0 CG B:HIS74 4.6 34.7 1.0 ND1 B:HIS149 4.6 31.2 1.0 ND1 B:HIS76 4.7 36.5 1.0 CA B:HIS76 4.7 31.9 1.0 CG B:ASP78 4.8 44.8 1.0

S.A.Sattler, X.Wang, K.M.Lewis, P.J.Dehan, C.M.Park, Y.Xin, H.Liu, M.Xian, L.Xun, C.Kang. Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-Beta-Lactamase Superfamily. J.Biol.Chem. V. 290 18914 2015.
ISSN: ESSN 1083-351X
PubMed: 26082492
DOI: 10.1074/JBC.M115.652537