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Iron in PDB 3fpw: Crystal Structure of Hbps with Bound Iron

Protein crystallography data

The structure of Crystal Structure of Hbps with Bound Iron, PDB code: 3fpw was solved by D.Ortiz De Orue Lucana, G.Bogel, P.Zou, M.R.Groves, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.80 / 1.60
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 77.940, 77.940, 79.990, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Hbps with Bound Iron (pdb code 3fpw). 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 Hbps with Bound Iron, PDB code: 3fpw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3fpw

Go back to Iron Binding Sites List in 3fpw
Iron binding site 1 out of 2 in the Crystal Structure of Hbps with Bound Iron


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 Hbps with Bound Iron within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe157

b:48.8
occ:0.25
NZ A:LYS108 3.5 28.7 1.0
O A:HOH261 3.8 40.6 1.0
CE A:LYS108 4.2 27.1 1.0
O A:HOH278 4.4 38.3 1.0
O A:HOH232 5.0 25.1 1.0

Iron binding site 2 out of 2 in 3fpw

Go back to Iron Binding Sites List in 3fpw
Iron binding site 2 out of 2 in the Crystal Structure of Hbps with Bound Iron


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 Hbps with Bound Iron within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe158

b:48.3
occ:0.50
O A:HOH291 3.6 44.7 1.0

Reference:

D.Ortiz De Orue Lucana, G.Bogel, P.Zou, M.R.Groves. The Oligomeric Assembly of the Novel Haem-Degrading Protein Hbps Is Essential For Interaction with Its Cognate Two-Component Sensor Kinase J.Mol.Biol. V. 386 1108 2009.
ISSN: ISSN 0022-2836
PubMed: 19244623
DOI: 10.1016/J.JMB.2009.01.017
Page generated: Sun Aug 4 10:18:42 2024

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