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Iron in PDB 4xmh: Crystal Structure of Nitrophorin 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly

Enzymatic activity of Crystal Structure of Nitrophorin 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly

All present enzymatic activity of Crystal Structure of Nitrophorin 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly:
1.7.6.1;

Protein crystallography data

The structure of Crystal Structure of Nitrophorin 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly, PDB code: 4xmh was solved by H.Ogata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.71 / 1.29
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.374, 66.929, 38.885, 90.00, 116.79, 90.00
R / Rfree (%) 15.5 / 18.2

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Nitrophorin 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly (pdb code 4xmh). 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 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly, PDB code: 4xmh:

Iron binding site 1 out of 1 in 4xmh

Go back to Iron Binding Sites List in 4xmh
Iron binding site 1 out of 1 in the Crystal Structure of Nitrophorin 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly


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 7 From Rhodnius Prolixus at pH 7.8 Complexed with Gly-Gly-Gly within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:14.1
occ:0.77
 FE A:HEM201 0.0 14.1 0.8
N B:GLY1 2.0 19.1 1.0
ND A:HEM201 2.0 13.9 0.8
NC A:HEM201 2.0 13.3 0.8
NA A:HEM201 2.0 16.4 0.8
NB A:HEM201 2.1 14.2 0.8
NE2 A:HIS60 2.2 16.9 1.0
CA B:GLY1 3.0 21.9 1.0
C4D A:HEM201 3.0 16.1 0.8
C4C A:HEM201 3.0 13.1 0.8
C1D A:HEM201 3.0 14.3 0.8
C1A A:HEM201 3.0 16.9 0.8
C1B A:HEM201 3.1 16.1 0.8
C1C A:HEM201 3.1 13.6 0.8
C4A A:HEM201 3.1 17.7 0.8
C4B A:HEM201 3.1 14.8 0.8
CD2 A:HIS60 3.1 15.4 1.0
CE1 A:HIS60 3.1 16.0 1.0
CHA A:HEM201 3.4 17.5 0.8
CHD A:HEM201 3.4 13.6 0.8
CHB A:HEM201 3.4 18.1 0.8
CHC A:HEM201 3.5 13.7 0.8
ND1 A:HIS60 4.2 14.8 1.0
CG A:HIS60 4.2 14.8 1.0
C3D A:HEM201 4.3 18.7 0.8
C2C A:HEM201 4.3 15.7 0.8
C2D A:HEM201 4.3 16.9 0.8
C3C A:HEM201 4.3 14.4 0.8
C2A A:HEM201 4.3 20.1 0.8
C3A A:HEM201 4.3 19.0 0.8
C2B A:HEM201 4.3 17.1 0.8
C3B A:HEM201 4.3 16.2 0.8
O B:HOH106 4.3 21.8 0.7
C B:GLY1 4.3 23.8 1.0
CD1 A:PHE43 4.8 13.4 1.0
O B:GLY1 4.8 26.1 1.0
CE1 A:PHE43 4.9 13.4 1.0

Reference:

M.Knipp, H.Ogata, G.Soavi, G.Cerullo, A.Allegri, S.Abbruzzetti, S.Bruno, C.Viappiani, A.Bidon-Chanal, F.J.Luque. Structure and Dynamics of the Membrane Attaching Nitric Oxide Transporter Nitrophorin 7. F1000RES V. 4 45 2015.
ISSN: ISSN 2046-1402
PubMed: 26167269
DOI: 10.12688/F1000RESEARCH.6060.1
Page generated: Tue Aug 5 17:11:45 2025

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