Iron in PDB 2acp: Crystal Structure of Nitrophorin 2 Aqua Complex

The structure of Crystal Structure of Nitrophorin 2 Aqua Complex, PDB code: 2acp was solved by A.Weichsel, R.E.Berry, F.A.Walker, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	39.754, 125.642, 33.468, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 23.3

The binding sites of Iron atom in the Crystal Structure of Nitrophorin 2 Aqua Complex (pdb code 2acp). 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 Aqua Complex, PDB code: 2acp:

Iron binding site 1 out of 1 in the Crystal Structure of Nitrophorin 2 Aqua Complex


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 Aqua Complex within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe201 b:22.0 occ:1.00 FE X:HEM201 0.0 22.0 1.0 NC X:HEM201 2.0 22.0 1.0 NA X:HEM201 2.1 25.3 1.0 NB X:HEM201 2.1 21.5 1.0 ND X:HEM201 2.1 22.4 1.0 NE2 X:HIS57 2.2 23.2 1.0 O X:HOH181 2.3 35.6 1.0 C1C X:HEM201 3.0 21.2 1.0 C1A X:HEM201 3.0 23.2 1.0 C4B X:HEM201 3.1 20.5 1.0 C1D X:HEM201 3.1 23.1 1.0 C4A X:HEM201 3.1 25.6 1.0 C4C X:HEM201 3.1 22.5 1.0 C4D X:HEM201 3.1 22.7 1.0 C1B X:HEM201 3.1 22.7 1.0 CE1 X:HIS57 3.1 22.6 1.0 CD2 X:HIS57 3.2 21.8 1.0 CHA X:HEM201 3.4 25.8 1.0 CHC X:HEM201 3.4 22.5 1.0 CHB X:HEM201 3.4 25.1 1.0 CHD X:HEM201 3.4 22.6 1.0 C2C X:HEM201 4.2 22.2 1.0 C2B X:HEM201 4.2 23.2 1.0 C3C X:HEM201 4.3 21.8 1.0 C3B X:HEM201 4.3 21.8 1.0 C2A X:HEM201 4.3 28.1 1.0 C2D X:HEM201 4.3 24.7 1.0 C3A X:HEM201 4.3 28.5 1.0 ND1 X:HIS57 4.3 23.5 1.0 C3D X:HEM201 4.3 26.6 1.0 CG X:HIS57 4.3 22.4 1.0 CD2 X:LEU132 4.6 21.7 1.0

A.Weichsel, R.E.Berry, F.A.Walker, W.R.Montfort. Crystal Structures, Ligand Induced Conformational Change and Heme Deformation in Complexes of Nitrophorin 2, A Nitric Oxide Transport Protein From Rhodnius Prolixus To Be Published.