Iron in PDB 2amm: Crystal Structure of L122V/L132V Mutant of Nitrophorin 2

The structure of Crystal Structure of L122V/L132V Mutant of Nitrophorin 2, PDB code: 2amm 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)	18.00 / 1.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	34.147, 34.147, 256.223, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 22.1

The binding sites of Iron atom in the Crystal Structure of L122V/L132V Mutant of Nitrophorin 2 (pdb code 2amm). 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 L122V/L132V Mutant of Nitrophorin 2, PDB code: 2amm:

Iron binding site 1 out of 1 in the Crystal Structure of L122V/L132V Mutant of Nitrophorin 2


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 L122V/L132V Mutant of Nitrophorin 2 within 5.0Å range: probe atom residue distance (Å) B Occ X:Fe201 b:6.5 occ:1.00 FE X:HEM201 0.0 6.5 1.0 NA X:HEM201 2.0 6.7 1.0 NB X:HEM201 2.0 3.3 1.0 NC X:HEM201 2.0 3.0 1.0 ND X:HEM201 2.0 6.5 1.0 NE2 X:HIS57 2.1 4.5 1.0 O X:HOH460 2.1 7.5 1.0 CE1 X:HIS57 3.0 3.6 1.0 C1A X:HEM201 3.0 7.4 1.0 C4B X:HEM201 3.0 5.1 1.0 C4D X:HEM201 3.0 7.2 1.0 C1D X:HEM201 3.0 6.2 1.0 C1B X:HEM201 3.0 4.4 1.0 C4A X:HEM201 3.1 7.8 1.0 C1C X:HEM201 3.1 5.2 1.0 C4C X:HEM201 3.1 5.4 1.0 CD2 X:HIS57 3.1 7.0 1.0 CHA X:HEM201 3.3 6.7 1.0 CHC X:HEM201 3.4 6.4 1.0 CHD X:HEM201 3.4 5.4 1.0 CHB X:HEM201 3.4 7.3 1.0 O X:HOH502 4.1 7.0 1.0 ND1 X:HIS57 4.1 6.4 1.0 C3B X:HEM201 4.2 6.1 1.0 CG X:HIS57 4.2 5.2 1.0 C2B X:HEM201 4.2 4.0 1.0 C2A X:HEM201 4.2 8.2 1.0 C3D X:HEM201 4.2 5.1 1.0 C2D X:HEM201 4.3 5.7 1.0 C3C X:HEM201 4.3 4.4 1.0 C2C X:HEM201 4.3 4.2 1.0 C3A X:HEM201 4.3 7.9 1.0 CG2 X:VAL122 5.0 7.9 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.