Iron in PDB 1sxy: 1.07 A Crystal Structure of D30N Mutant of Nitrophorin 4 From Rhodnius Prolixus

The structure of 1.07 A Crystal Structure of D30N Mutant of Nitrophorin 4 From Rhodnius Prolixus, PDB code: 1sxy was solved by E.M.Maes, A.Weichsel, J.F.Andersen, D.Shepley, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.80 / 1.07
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.142, 42.776, 52.979, 90.00, 94.05, 90.00
R / Rfree (%)	15 / 17.2

The binding sites of Iron atom in the 1.07 A Crystal Structure of D30N Mutant of Nitrophorin 4 From Rhodnius Prolixus (pdb code 1sxy). 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 1.07 A Crystal Structure of D30N Mutant of Nitrophorin 4 From Rhodnius Prolixus, PDB code: 1sxy:

Iron binding site 1 out of 1 in the 1.07 A Crystal Structure of D30N Mutant of Nitrophorin 4 From Rhodnius Prolixus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.07 A Crystal Structure of D30N Mutant of Nitrophorin 4 From Rhodnius Prolixus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe185 b:6.0 occ:1.00 FE A:HEM185 0.0 6.0 1.0 NB A:HEM185 2.0 5.8 1.0 NC A:HEM185 2.0 6.6 1.0 NA A:HEM185 2.0 6.4 1.0 ND A:HEM185 2.0 6.6 1.0 NE2 A:HIS59 2.0 5.8 1.0 N A:NH4200 2.0 8.6 1.0 CE1 A:HIS59 3.0 5.2 1.0 CD2 A:HIS59 3.0 5.8 1.0 C4C A:HEM185 3.0 7.2 1.0 C1B A:HEM185 3.0 6.9 1.0 C1A A:HEM185 3.0 6.7 1.0 C1C A:HEM185 3.0 7.1 1.0 C1D A:HEM185 3.0 8.2 1.0 C4A A:HEM185 3.0 6.9 1.0 C4D A:HEM185 3.0 7.6 1.0 C4B A:HEM185 3.0 6.7 1.0 CHB A:HEM185 3.4 7.0 1.0 CHC A:HEM185 3.4 6.9 1.0 CHD A:HEM185 3.4 7.7 1.0 CHA A:HEM185 3.4 7.5 1.0 ND1 A:HIS59 4.1 5.4 1.0 CG A:HIS59 4.1 5.8 1.0 C3C A:HEM185 4.2 7.8 1.0 C2C A:HEM185 4.2 7.2 1.0 C2A A:HEM185 4.2 7.5 1.0 C3B A:HEM185 4.2 7.3 1.0 C3A A:HEM185 4.3 7.3 1.0 C3D A:HEM185 4.3 8.8 1.0 C2B A:HEM185 4.3 6.8 1.0 C2D A:HEM185 4.3 10.0 1.0 O A:HOH240 4.7 15.1 1.0 CD2 A:LEU133 4.8 11.7 1.0

E.M.Maes, A.Weichsel, J.F.Andersen, D.Shepley, W.R.Montfort. Role of Binding Site Loops in Controlling Nitric Oxide Release: Structure and Kinetics of Mutant Forms of Nitrophorin 4 Biochemistry V. 43 6679 2004.
ISSN: ISSN 0006-2960
PubMed: 15157102
DOI: 10.1021/BI049748A