Iron in PDB 5ocb: Crystal Structure of Nitric Oxide Bound D97N Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

The structure of Crystal Structure of Nitric Oxide Bound D97N Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 5ocb was solved by J.Dong, D.Sasaki, R.Eady, S.V.Antonyuk, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.61 / 1.78
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	180.460, 180.460, 180.460, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 16.2

The structure of Crystal Structure of Nitric Oxide Bound D97N Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Iron atom in the Crystal Structure of Nitric Oxide Bound D97N Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii (pdb code 5ocb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Nitric Oxide Bound D97N Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 5ocb:

Iron binding site 1 out of 1 in the Crystal Structure of Nitric Oxide Bound D97N Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii


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 Nitric Oxide Bound D97N Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe503 b:24.9 occ:1.00 FE A:HEC503 0.0 24.9 1.0 ND A:HEC503 1.9 28.3 1.0 NA A:HEC503 2.0 27.3 1.0 NE2 A:HIS368 2.1 26.2 1.0 NB A:HEC503 2.1 25.1 1.0 NC A:HEC503 2.1 23.9 1.0 SD A:MET418 2.2 25.7 1.0 C4D A:HEC503 3.0 28.1 1.0 C1D A:HEC503 3.0 25.8 1.0 CE1 A:HIS368 3.0 26.9 1.0 C4B A:HEC503 3.0 25.6 1.0 C1A A:HEC503 3.0 27.7 1.0 C4A A:HEC503 3.0 28.5 1.0 C1B A:HEC503 3.0 27.4 1.0 C4C A:HEC503 3.1 24.8 1.0 C1C A:HEC503 3.1 24.4 1.0 CD2 A:HIS368 3.1 26.4 1.0 CG A:MET418 3.4 25.2 1.0 CHA A:HEC503 3.4 26.7 1.0 CE A:MET418 3.4 24.7 1.0 CHC A:HEC503 3.4 24.1 1.0 CHD A:HEC503 3.4 25.6 1.0 CHB A:HEC503 3.4 26.8 1.0 CB A:MET418 4.1 25.8 1.0 ND1 A:HIS368 4.1 25.8 1.0 CG A:HIS368 4.2 25.4 1.0 C2D A:HEC503 4.2 26.8 1.0 C3D A:HEC503 4.2 27.1 1.0 C2A A:HEC503 4.2 29.2 1.0 C3A A:HEC503 4.2 29.2 1.0 C2B A:HEC503 4.3 26.2 1.0 C3B A:HEC503 4.3 25.3 1.0 C2C A:HEC503 4.3 24.3 1.0 C3C A:HEC503 4.3 24.8 1.0

J.Dong, D.Sasaki, R.Eady, S.V.Antonyuk, S.S.Hasnain. Activation of Redox Tyrosine Switch Is Required For Ligand Binding at the Catalytic Site in Heme-Cu Nitrite Reductases To Be Published.