Iron in PDB 1jmx: Crystal Structure of A Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida

The structure of Crystal Structure of A Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida, PDB code: 1jmx was solved by A.Satoh, I.Miyahara, K.Hirotsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	167.210, 92.370, 79.300, 90.00, 112.00, 90.00
R / Rfree (%)	20.9 / 26.7

The structure of Crystal Structure of A Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Iron atom in the Crystal Structure of A Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida (pdb code 1jmx). 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 A Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida, PDB code: 1jmx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of A Quinohemoprotein Amine Dehydrogenase 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 A Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:10.6 occ:1.00 FE A:HEC1001 0.0 10.6 1.0 NB A:HEC1001 1.9 10.2 1.0 NA A:HEC1001 2.0 10.7 1.0 ND A:HEC1001 2.0 10.1 1.0 NC A:HEC1001 2.0 10.3 1.0 NE2 A:HIS104 2.0 10.7 1.0 NE2 A:HIS126 2.1 10.0 1.0 CD2 A:HIS104 2.9 8.4 1.0 C4D A:HEC1001 3.0 11.1 1.0 C1A A:HEC1001 3.0 10.1 1.0 C4A A:HEC1001 3.0 11.0 1.0 C1B A:HEC1001 3.0 9.9 1.0 C1C A:HEC1001 3.0 9.2 1.0 C4B A:HEC1001 3.0 8.9 1.0 CD2 A:HIS126 3.0 7.8 1.0 C4C A:HEC1001 3.0 9.2 1.0 C1D A:HEC1001 3.0 9.7 1.0 CE1 A:HIS104 3.1 6.3 1.0 CE1 A:HIS126 3.1 9.1 1.0 CHA A:HEC1001 3.3 10.6 1.0 CHB A:HEC1001 3.4 9.8 1.0 CHC A:HEC1001 3.4 9.1 1.0 CHD A:HEC1001 3.4 8.4 1.0 CG A:HIS104 4.1 8.9 1.0 ND1 A:HIS104 4.2 7.5 1.0 CG A:HIS126 4.2 9.6 1.0 ND1 A:HIS126 4.2 9.5 1.0 C3D A:HEC1001 4.2 11.6 1.0 C2A A:HEC1001 4.2 11.2 1.0 C3A A:HEC1001 4.2 11.6 1.0 C2C A:HEC1001 4.3 8.8 1.0 C3B A:HEC1001 4.3 9.7 1.0 C2B A:HEC1001 4.3 8.6 1.0 C3C A:HEC1001 4.3 9.6 1.0 C2D A:HEC1001 4.3 8.6 1.0 O A:HOH2013 4.7 8.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of A Quinohemoprotein Amine Dehydrogenase 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 A Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1002 b:11.7 occ:1.00 FE A:HEC1002 0.0 11.7 1.0 NA A:HEC1002 2.0 11.1 1.0 NB A:HEC1002 2.0 10.2 1.0 NC A:HEC1002 2.0 11.6 1.0 ND A:HEC1002 2.0 9.7 1.0 NE2 A:HIS16 2.0 8.4 1.0 SD A:MET44 2.5 12.5 1.0 CE1 A:HIS16 3.0 8.7 1.0 C1A A:HEC1002 3.0 11.7 1.0 C4A A:HEC1002 3.0 10.3 1.0 C4D A:HEC1002 3.0 8.5 1.0 C1B A:HEC1002 3.0 8.9 1.0 C4B A:HEC1002 3.0 10.2 1.0 C1C A:HEC1002 3.0 12.2 1.0 C4C A:HEC1002 3.0 11.2 1.0 C1D A:HEC1002 3.1 9.4 1.0 CD2 A:HIS16 3.1 7.3 1.0 CHA A:HEC1002 3.4 10.2 1.0 CHB A:HEC1002 3.4 10.0 1.0 CHC A:HEC1002 3.4 9.8 1.0 CHD A:HEC1002 3.4 10.7 1.0 CG A:MET44 3.5 10.1 1.0 CE A:MET44 3.6 8.9 1.0 ND1 A:HIS16 4.1 9.8 1.0 CG A:HIS16 4.2 9.2 1.0 C3A A:HEC1002 4.2 11.5 1.0 C2A A:HEC1002 4.3 11.3 1.0 C3B A:HEC1002 4.3 9.8 1.0 C3D A:HEC1002 4.3 8.7 1.0 C2B A:HEC1002 4.3 9.2 1.0 C2C A:HEC1002 4.3 13.1 1.0 C3C A:HEC1002 4.3 13.3 1.0 C2D A:HEC1002 4.3 9.8 1.0 CB A:MET44 4.6 11.5 1.0

A.Satoh, J.K.Kim, I.Miyahara, B.Devreese, I.Vandenberghe, A.Hacisalihoglu, T.Okajima, S.Kuroda, O.Adachi, J.A.Duine, J.Van Beeumen, K.Tanizawa, K.Hirotsu. Crystal Structure of Quinohemoprotein Amine Dehydrogenase From Pseudomonas Putida. Identification of A Novel Quinone Cofactor Encaged By Multiple Thioether Cross-Bridges. J.Biol.Chem. V. 277 2830 2002.
ISSN: ISSN 0021-9258
PubMed: 11704672
DOI: 10.1074/JBC.M109090200