Iron in PDB 1x8o: 1.01 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6

The structure of 1.01 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6, PDB code: 1x8o was solved by D.A.Kondrashov, S.A.Roberts, A.Weichsel, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.01
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.445, 42.729, 53.098, 90.00, 94.43, 90.00
R / Rfree (%)	10.2 / 13

The binding sites of Iron atom in the 1.01 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 (pdb code 1x8o). 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 1.01 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6, PDB code: 1x8o:

Iron binding site 1 out of 1 in the 1.01 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.01 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:4.0 occ:1.00 FE A:HEM202 0.0 4.0 1.0 N A:NO203 1.7 5.5 1.0 NA A:HEM202 2.0 4.2 0.6 ND A:HEM202 2.0 4.2 0.4 NA A:HEM202 2.0 4.5 0.4 ND A:HEM202 2.0 4.5 0.6 NE2 A:HIS59 2.0 3.6 1.0 NC A:HEM202 2.0 4.7 0.4 NB A:HEM202 2.0 4.7 0.6 NC A:HEM202 2.0 4.5 0.6 NB A:HEM202 2.0 4.5 0.4 O A:NO203 2.7 9.3 1.0 CE1 A:HIS59 3.0 3.6 1.0 C1B A:HEM202 3.0 4.5 0.6 C4C A:HEM202 3.0 4.5 0.4 C4D A:HEM202 3.0 4.8 0.6 C1A A:HEM202 3.0 4.8 0.4 C1C A:HEM202 3.0 4.5 0.6 C4B A:HEM202 3.0 4.5 0.4 C4A A:HEM202 3.0 5.5 0.4 C1D A:HEM202 3.0 5.5 0.6 CD2 A:HIS59 3.0 3.7 1.0 C4A A:HEM202 3.0 4.0 0.6 C1D A:HEM202 3.0 4.0 0.4 C1B A:HEM202 3.0 5.1 0.4 C4C A:HEM202 3.0 5.1 0.6 C4D A:HEM202 3.0 4.1 0.4 C1A A:HEM202 3.0 4.1 0.6 C1C A:HEM202 3.0 4.8 0.4 C4B A:HEM202 3.0 4.8 0.6 CHB A:HEM202 3.4 4.5 0.6 CHD A:HEM202 3.4 4.5 0.4 CHC A:HEM202 3.4 5.2 1.0 CHA A:HEM202 3.4 4.4 1.0 CHB A:HEM202 3.4 5.4 0.4 CHD A:HEM202 3.4 5.4 0.6 ND1 A:HIS59 4.1 3.5 1.0 CG A:HIS59 4.2 3.2 1.0 C2D A:HEM202 4.2 4.1 0.4 C3A A:HEM202 4.2 4.1 0.6 C2D A:HEM202 4.3 6.5 0.6 C3A A:HEM202 4.3 6.5 0.4 C2A A:HEM202 4.3 6.2 0.4 C3D A:HEM202 4.3 6.2 0.6 C3C A:HEM202 4.3 5.0 0.4 C2B A:HEM202 4.3 5.0 0.6 C3B A:HEM202 4.3 5.5 0.6 C2C A:HEM202 4.3 5.5 0.4 C2A A:HEM202 4.3 4.3 0.6 C3D A:HEM202 4.3 4.3 0.4 C3B A:HEM202 4.3 5.7 0.4 C2C A:HEM202 4.3 5.7 0.6 C3C A:HEM202 4.3 5.6 0.6 C2B A:HEM202 4.3 5.6 0.4 CD2 A:LEU133 4.6 8.7 1.0 CD2 A:LEU130 4.7 12.0 0.7 CD2 A:LEU123 4.9 6.8 1.0

D.A.Kondrashov, S.A.Roberts, A.Weichsel, W.R.Montfort. Protein Functional Cycle Viewed at Atomic Resolution: Conformational Change and Mobility in Nitrophorin 4 As A Function of pH and No Binding Biochemistry V. 43 13637 2004.
ISSN: ISSN 0006-2960
PubMed: 15504026
DOI: 10.1021/BI0483155