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Iron in PDB 2ofr: 1.00 A Crystal Structure of V36A/D129A/L130A Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6

Protein crystallography data

The structure of 1.00 A Crystal Structure of V36A/D129A/L130A Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6, PDB code: 2ofr was solved by A.M.Amoia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.47 / 1.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.191, 42.637, 52.975, 90.00, 94.12, 90.00
R / Rfree (%) 12.6 / 14.8

Iron Binding Sites:

The binding sites of Iron atom in the 1.00 A Crystal Structure of V36A/D129A/L130A Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6 (pdb code 2ofr). 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 1.00 A Crystal Structure of V36A/D129A/L130A Mutant of Nitrophorin 4 From Rhodnius Prolixus Complexed with Nitric Oxide at pH 5.6, PDB code: 2ofr:

Iron binding site 1 out of 1 in 2ofr

Go back to Iron Binding Sites List in 2ofr
Iron binding site 1 out of 1 in the 1.00 A Crystal Structure of V36A/D129A/L130A Mutant 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 1.00 A Crystal Structure of V36A/D129A/L130A Mutant 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
X:Fe185

b:5.6
occ:1.00
FE X:HEM185 0.0 5.6 1.0
N X:NO186 1.7 7.3 1.0
NB X:HEM185 2.0 5.7 1.0
NC X:HEM185 2.0 5.9 1.0
ND X:HEM185 2.0 6.7 1.0
NA X:HEM185 2.0 5.7 1.0
NE2 X:HIS59 2.0 5.4 1.0
O X:NO186 2.8 15.2 1.0
C1C X:HEM185 3.0 6.8 1.0
CE1 X:HIS59 3.0 5.2 1.0
C4B X:HEM185 3.0 6.3 1.0
C1B X:HEM185 3.0 5.8 1.0
C4D X:HEM185 3.0 6.7 1.0
C4C X:HEM185 3.0 6.8 1.0
C1A X:HEM185 3.0 6.5 1.0
C1D X:HEM185 3.0 7.2 1.0
C4A X:HEM185 3.0 5.7 1.0
CD2 X:HIS59 3.0 5.5 1.0
CHB X:HEM185 3.4 6.3 1.0
CHD X:HEM185 3.4 7.7 1.0
CHC X:HEM185 3.4 7.0 1.0
CHA X:HEM185 3.4 6.8 1.0
ND1 X:HIS59 4.1 5.3 1.0
CG X:HIS59 4.2 5.5 1.0
C2C X:HEM185 4.2 7.5 1.0
C3B X:HEM185 4.2 7.8 1.0
O X:HOH320 4.2 23.3 1.0
C2B X:HEM185 4.2 6.7 1.0
C3C X:HEM185 4.2 7.7 1.0
C3A X:HEM185 4.2 6.6 1.0
C2A X:HEM185 4.3 6.2 1.0
C2D X:HEM185 4.3 9.5 1.0
C3D X:HEM185 4.3 8.8 1.0
CD2 X:LEU133 4.7 9.0 0.5
CD2 X:LEU123 5.0 9.3 1.0

Reference:

A.M.Amoia, W.R.Montfort. Ligand Protection and Nitric Oxide Interactions with Heme in Nitrophorin 4: Kinetic and Structural Analyses of A Loop Mutant To Be Published.
Page generated: Sun Dec 13 14:50:18 2020

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