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Iron in PDB 1ike: Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Histamine at 1.5 A Resolution

Protein crystallography data

The structure of Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Histamine at 1.5 A Resolution, PDB code: 1ike was solved by S.A.Roberts, A.Weichsel, Y.Qiu, J.A.Shelnutt, 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) 8.90 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.180, 42.520, 52.860, 90.00, 94.35, 90.00
R / Rfree (%) 18 / 24

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Histamine at 1.5 A Resolution (pdb code 1ike). 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 4 From Rhodnius Prolixus Complexed with Histamine at 1.5 A Resolution, PDB code: 1ike:

Iron binding site 1 out of 1 in 1ike

Go back to Iron Binding Sites List in 1ike
Iron binding site 1 out of 1 in the Crystal Structure of Nitrophorin 4 From Rhodnius Prolixus Complexed with Histamine at 1.5 A Resolution


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 4 From Rhodnius Prolixus Complexed with Histamine at 1.5 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe185

b:12.8
occ:1.00
FE A:HEM185 0.0 12.8 1.0
ND A:HEM185 2.0 9.6 0.5
NA A:HEM185 2.0 9.6 0.5
NE2 A:HIS59 2.0 10.1 1.0
NB A:HEM185 2.0 13.1 0.5
NC A:HEM185 2.0 13.1 0.5
ND A:HEM185 2.0 11.9 0.5
NA A:HEM185 2.0 11.9 0.5
NE2 A:HSM190 2.0 12.3 1.0
NB A:HEM185 2.1 11.4 0.5
NC A:HEM185 2.1 11.4 0.5
CD2 A:HIS59 2.9 9.4 1.0
CD2 A:HSM190 2.9 14.6 1.0
C1A A:HEM185 3.0 13.3 0.5
C4D A:HEM185 3.0 13.3 0.5
CE1 A:HIS59 3.0 10.5 1.0
C1D A:HEM185 3.0 8.1 0.5
C4A A:HEM185 3.0 8.1 0.5
C1A A:HEM185 3.0 17.4 0.5
C4D A:HEM185 3.0 17.4 0.5
C1C A:HEM185 3.0 10.0 0.5
C4B A:HEM185 3.0 10.0 0.5
C1B A:HEM185 3.0 12.1 0.5
C4C A:HEM185 3.0 12.1 0.5
C1D A:HEM185 3.1 17.8 0.5
C4A A:HEM185 3.1 17.8 0.5
C1B A:HEM185 3.1 10.9 0.5
C4C A:HEM185 3.1 10.9 0.5
C1C A:HEM185 3.1 8.8 0.5
C4B A:HEM185 3.1 8.8 0.5
CE1 A:HSM190 3.1 17.2 1.0
CHA A:HEM185 3.3 10.9 1.0
CHB A:HEM185 3.4 13.8 0.5
CHD A:HEM185 3.4 14.0 0.5
CHC A:HEM185 3.4 10.4 1.0
CG A:HIS59 4.1 11.4 1.0
ND1 A:HIS59 4.1 9.3 1.0
CG A:HSM190 4.2 16.2 1.0
C2A A:HEM185 4.2 13.2 0.5
C3D A:HEM185 4.2 13.2 0.5
ND1 A:HSM190 4.2 12.4 1.0
C3A A:HEM185 4.2 10.6 0.5
C2D A:HEM185 4.2 10.6 0.5
C2A A:HEM185 4.2 16.2 0.5
C3D A:HEM185 4.2 16.2 0.5
C3B A:HEM185 4.3 11.9 0.5
C2C A:HEM185 4.3 11.9 0.5
C3A A:HEM185 4.3 21.5 0.5
C2D A:HEM185 4.3 21.5 0.5
C2B A:HEM185 4.3 11.6 0.5
C3C A:HEM185 4.3 11.6 0.5
C3B A:HEM185 4.3 15.3 0.5
C2C A:HEM185 4.3 15.3 0.5
C2B A:HEM185 4.3 13.2 0.5
C3C A:HEM185 4.3 13.2 0.5
CD2 A:LEU123 5.0 12.8 1.0

Reference:

S.A.Roberts, A.Weichsel, Y.Qiu, J.A.Shelnutt, F.A.Walker, W.R.Montfort. Ligand-Induced Heme Ruffling and Bent No Geometry in Ultra-High-Resolution Structures of Nitrophorin 4. Biochemistry V. 40 11327 2001.
ISSN: ISSN 0006-2960
PubMed: 11560480
DOI: 10.1021/BI0109257
Page generated: Sun Dec 13 14:18:32 2020

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