Iron in PDB 1jju: Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking

The structure of Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking, PDB code: 1jju was solved by S.Datta, Y.Mori, K.Takagi, K.Kawaguchi, Z.-W.Chen, K.Kano, T.Ikeda, T.Okajima, S.Kuroda, K.Tanizawa, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.05
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.489, 99.489, 214.489, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 25.1

The structure of Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Iron atom in the Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking (pdb code 1jju). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking, PDB code: 1jju:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe991 b:31.6 occ:1.00 FE A:HEM991 0.0 31.6 1.0 ND A:HEM991 2.0 28.3 1.0 NC A:HEM991 2.0 21.6 1.0 NB A:HEM991 2.0 31.4 1.0 NA A:HEM991 2.0 26.1 1.0 NE2 A:HIS15 2.1 31.4 1.0 SD A:MET43 2.4 27.8 1.0 C4D A:HEM991 3.0 26.2 1.0 C1A A:HEM991 3.0 27.9 1.0 C1C A:HEM991 3.0 32.5 1.0 C1D A:HEM991 3.0 28.3 1.0 C1B A:HEM991 3.1 28.6 1.0 C4C A:HEM991 3.1 30.9 1.0 C4A A:HEM991 3.1 29.3 1.0 C4B A:HEM991 3.1 30.1 1.0 CD2 A:HIS15 3.1 28.7 1.0 CE1 A:HIS15 3.1 31.9 1.0 CHA A:HEM991 3.4 22.6 1.0 CHD A:HEM991 3.4 26.4 1.0 CHB A:HEM991 3.4 27.7 1.0 CHC A:HEM991 3.4 29.9 1.0 CG A:MET43 3.5 22.9 1.0 CE A:MET43 3.6 29.7 1.0 CG A:HIS15 4.1 36.3 1.0 C3D A:HEM991 4.3 31.0 1.0 C2A A:HEM991 4.3 26.2 1.0 C2D A:HEM991 4.3 32.3 1.0 ND1 A:HIS15 4.3 37.0 1.0 C3A A:HEM991 4.3 26.7 1.0 C3B A:HEM991 4.3 30.9 1.0 C2B A:HEM991 4.3 30.4 1.0 C2C A:HEM991 4.3 33.1 1.0 C3C A:HEM991 4.3 30.4 1.0 CB A:MET43 4.6 28.4 1.0

Iron binding site 2 out of 2 in the Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe992 b:30.8 occ:1.00 FE A:HEM992 0.0 30.8 1.0 ND A:HEM992 2.0 24.2 1.0 NB A:HEM992 2.0 29.2 1.0 NC A:HEM992 2.0 27.2 1.0 NA A:HEM992 2.0 29.1 1.0 NE2 A:HIS126 2.0 32.9 1.0 NE2 A:HIS104 2.1 31.3 1.0 CD2 A:HIS126 3.0 34.8 1.0 C4D A:HEM992 3.0 28.3 1.0 C1D A:HEM992 3.0 26.5 1.0 C1A A:HEM992 3.1 27.0 1.0 C1B A:HEM992 3.1 31.5 1.0 C1C A:HEM992 3.1 28.3 1.0 C4B A:HEM992 3.1 32.5 1.0 C4A A:HEM992 3.1 27.9 1.0 C4C A:HEM992 3.1 23.8 1.0 CD2 A:HIS104 3.1 30.7 1.0 CE1 A:HIS104 3.2 31.6 1.0 CE1 A:HIS126 3.2 36.3 1.0 CHA A:HEM992 3.4 23.9 1.0 CHD A:HEM992 3.4 24.4 1.0 CHB A:HEM992 3.4 30.2 1.0 CHC A:HEM992 3.4 23.5 1.0 CG A:HIS126 4.1 34.6 1.0 CG A:HIS104 4.2 27.7 1.0 C3D A:HEM992 4.3 26.7 1.0 C2D A:HEM992 4.3 25.4 1.0 C3B A:HEM992 4.3 32.4 1.0 C2B A:HEM992 4.3 33.1 1.0 C3A A:HEM992 4.3 28.3 1.0 C2A A:HEM992 4.3 27.5 1.0 C3C A:HEM992 4.3 25.4 1.0 C2C A:HEM992 4.3 24.9 1.0 ND1 A:HIS126 4.3 33.5 1.0 ND1 A:HIS104 4.3 32.9 1.0 O A:HOH1018 4.6 23.9 1.0

S.Datta, Y.Mori, K.Takagi, K.Kawaguchi, Z.W.Chen, T.Okajima, S.Kuroda, T.Ikeda, K.Kano, K.Tanizawa, F.S.Mathews. Structure of A Quinohemoprotein Amine Dehydrogenase with An Uncommon Redox Cofactor and Highly Unusual Crosslinking. Proc.Natl.Acad.Sci.Usa V. 98 14268 2001.
ISSN: ISSN 0027-8424
PubMed: 11717396
DOI: 10.1073/PNAS.241429098