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Iron in PDB 1np1: Crystal Structure of the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine

Protein crystallography data

The structure of Crystal Structure of the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine, PDB code: 1np1 was solved by A.Weichsel, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.550, 74.570, 66.560, 90.00, 99.94, 90.00
R / Rfree (%) 18.1 / 27.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine (pdb code 1np1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine, PDB code: 1np1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1np1

Go back to Iron Binding Sites List in 1np1
Iron binding site 1 out of 2 in the Crystal Structure of the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine


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 the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe302

b:20.3
occ:1.00
FE A:HEM302 0.0 20.3 1.0
NC A:HEM302 1.9 15.0 1.0
NA A:HEM302 1.9 18.9 1.0
NE2 A:HIS59 2.0 13.9 1.0
NB A:HEM302 2.1 21.1 1.0
ND A:HEM302 2.1 21.6 1.0
NE2 A:HSM303 2.1 23.6 1.0
CE1 A:HIS59 2.8 18.1 1.0
C4C A:HEM302 3.0 21.6 1.0
C1C A:HEM302 3.0 17.8 1.0
C1A A:HEM302 3.0 18.0 1.0
CE1 A:HSM303 3.0 26.7 1.0
C4A A:HEM302 3.1 19.6 1.0
C1D A:HEM302 3.1 16.6 1.0
CD2 A:HIS59 3.1 18.3 1.0
C4D A:HEM302 3.1 18.7 1.0
C4B A:HEM302 3.1 19.8 1.0
C1B A:HEM302 3.1 19.1 1.0
CD2 A:HSM303 3.2 29.0 1.0
CHA A:HEM302 3.4 17.4 1.0
CHC A:HEM302 3.4 15.9 1.0
CHD A:HEM302 3.4 18.3 1.0
CHB A:HEM302 3.5 17.3 1.0
ND1 A:HIS59 4.0 18.4 1.0
CG A:HIS59 4.2 19.5 1.0
C2A A:HEM302 4.2 18.6 1.0
ND1 A:HSM303 4.2 30.4 1.0
C2C A:HEM302 4.2 16.1 1.0
C3A A:HEM302 4.2 15.7 1.0
C3C A:HEM302 4.3 21.5 1.0
CG A:HSM303 4.3 30.0 1.0
C3D A:HEM302 4.4 19.9 1.0
C2B A:HEM302 4.4 14.9 1.0
C2D A:HEM302 4.4 18.2 1.0
C3B A:HEM302 4.4 17.2 1.0
CD2 A:LEU123 4.9 14.4 1.0

Iron binding site 2 out of 2 in 1np1

Go back to Iron Binding Sites List in 1np1
Iron binding site 2 out of 2 in the Crystal Structure of the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Complex of Nitrophorin 1 From Rhodnius Prolixus with Histamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe303

b:20.9
occ:1.00
FE B:HEM303 0.0 20.9 1.0
NB B:HEM303 1.9 19.1 1.0
ND B:HEM303 1.9 20.3 1.0
NA B:HEM303 2.0 21.2 1.0
NE2 B:HIS59 2.0 17.3 1.0
NC B:HEM303 2.0 19.8 1.0
NE2 B:HSM304 2.0 23.5 1.0
CE1 B:HSM304 2.9 26.0 1.0
CE1 B:HIS59 2.9 17.9 1.0
C4B B:HEM303 3.0 21.0 1.0
C4D B:HEM303 3.0 23.4 1.0
C1A B:HEM303 3.0 20.1 1.0
C1B B:HEM303 3.0 19.6 1.0
C4A B:HEM303 3.0 19.6 1.0
C1C B:HEM303 3.0 17.4 1.0
C1D B:HEM303 3.1 23.3 1.0
CD2 B:HIS59 3.1 15.1 1.0
C4C B:HEM303 3.1 19.8 1.0
CD2 B:HSM304 3.2 27.3 1.0
CHC B:HEM303 3.4 20.1 1.0
CHA B:HEM303 3.4 17.8 1.0
CHB B:HEM303 3.5 19.3 1.0
CHD B:HEM303 3.5 17.6 1.0
ND1 B:HSM304 4.1 23.6 1.0
ND1 B:HIS59 4.1 18.1 1.0
CG B:HIS59 4.2 17.8 1.0
C2B B:HEM303 4.2 17.0 1.0
C3D B:HEM303 4.2 24.0 1.0
C3B B:HEM303 4.2 20.8 1.0
C2D B:HEM303 4.2 21.1 1.0
C3A B:HEM303 4.3 17.0 1.0
CG B:HSM304 4.3 29.1 1.0
C2A B:HEM303 4.3 21.3 1.0
C2C B:HEM303 4.4 20.4 1.0
C3C B:HEM303 4.4 24.4 1.0

Reference:

A.Weichsel, J.F.Andersen, D.E.Champagne, F.A.Walker, W.R.Montfort. Crystal Structures of A Nitric Oxide Transport Protein From A Blood-Sucking Insect. Nat.Struct.Biol. V. 5 304 1998.
ISSN: ISSN 1072-8368
PubMed: 9546222
DOI: 10.1038/NSB0498-304
Page generated: Wed Jul 16 18:51:18 2025

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