Iron in PDB 1euo: Crystal Structure of Nitrophorin 2 (Prolixin-S)

The structure of Crystal Structure of Nitrophorin 2 (Prolixin-S), PDB code: 1euo was solved by J.F.Andersen, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.20 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	40.340, 127.960, 33.720, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 24.6

The binding sites of Iron atom in the Crystal Structure of Nitrophorin 2 (Prolixin-S) (pdb code 1euo). 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 Nitrophorin 2 (Prolixin-S), PDB code: 1euo:

Iron binding site 1 out of 1 in the Crystal Structure of Nitrophorin 2 (Prolixin-S)


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 Nitrophorin 2 (Prolixin-S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe260 b:19.6 occ:1.00 FE A:HEM260 0.0 19.6 1.0 NC A:HEM260 2.0 18.4 1.0 ND A:HEM260 2.0 18.4 1.0 NA A:HEM260 2.0 20.4 1.0 NB A:HEM260 2.0 18.3 1.0 NE2 A:HIS57 2.0 18.5 1.0 N A:NH3261 2.1 26.3 1.0 CE1 A:HIS57 3.0 15.8 1.0 C1D A:HEM260 3.0 17.7 1.0 C4D A:HEM260 3.0 19.1 1.0 C4A A:HEM260 3.0 22.0 1.0 C1C A:HEM260 3.0 18.5 1.0 C4C A:HEM260 3.0 17.9 1.0 C1A A:HEM260 3.0 22.3 1.0 C4B A:HEM260 3.0 17.7 1.0 C1B A:HEM260 3.0 18.6 1.0 CD2 A:HIS57 3.1 17.8 1.0 CHD A:HEM260 3.3 17.2 1.0 CHA A:HEM260 3.4 20.2 1.0 CHC A:HEM260 3.4 17.7 1.0 CHB A:HEM260 3.4 20.5 1.0 ND1 A:HIS57 4.1 16.4 1.0 CG A:HIS57 4.2 16.3 1.0 C2D A:HEM260 4.2 18.1 1.0 C3D A:HEM260 4.2 20.8 1.0 C3A A:HEM260 4.3 24.3 1.0 C2A A:HEM260 4.3 24.8 1.0 C2C A:HEM260 4.3 17.8 1.0 C3C A:HEM260 4.3 18.4 1.0 C3B A:HEM260 4.3 16.7 1.0 C2B A:HEM260 4.3 18.0 1.0 CD2 A:LEU132 4.7 21.6 1.0 O A:HOH194 4.9 48.3 1.0

J.F.Andersen, W.R.Montfort. The Crystal Structure of Nitrophorin 2. A Trifunctional Antihemostatic Protein From the Saliva of Rhodnius Prolixus J.Biol.Chem. V. 275 30496 2000.
ISSN: ISSN 0021-9258
PubMed: 10884386
DOI: 10.1074/JBC.M002857200