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Iron in PDB 3pqi: Crystal Structure of the Bacteriophage PHI92 Membrane-Piercing Protein GP138

Protein crystallography data

The structure of Crystal Structure of the Bacteriophage PHI92 Membrane-Piercing Protein GP138, PDB code: 3pqi was solved by C.Browning, M.Shneider, P.G.Leiman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.61 / 2.64
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 65.144, 65.144, 329.375, 90.00, 90.00, 120.00
R / Rfree (%) 21.1 / 25

Other elements in 3pqi:

The structure of Crystal Structure of the Bacteriophage PHI92 Membrane-Piercing Protein GP138 also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Bacteriophage PHI92 Membrane-Piercing Protein GP138 (pdb code 3pqi). 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 the Bacteriophage PHI92 Membrane-Piercing Protein GP138, PDB code: 3pqi:

Iron binding site 1 out of 1 in 3pqi

Go back to Iron Binding Sites List in 3pqi
Iron binding site 1 out of 1 in the Crystal Structure of the Bacteriophage PHI92 Membrane-Piercing Protein GP138


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 Bacteriophage PHI92 Membrane-Piercing Protein GP138 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe246

b:57.8
occ:0.33
NE2 A:HIS223 2.4 64.1 1.0
NE2 A:HIS225 2.4 65.3 1.0
CD2 A:HIS225 2.9 64.2 1.0
CE1 A:HIS223 3.3 63.5 1.0
CD2 A:HIS223 3.3 61.7 1.0
CE1 A:HIS225 3.7 65.9 1.0
CG A:HIS225 4.2 68.6 1.0
ND1 A:HIS223 4.4 63.4 1.0
CG A:HIS223 4.5 58.7 1.0
ND1 A:HIS225 4.5 68.9 1.0

Reference:

C.Browning, M.M.Shneider, V.D.Bowman, D.Schwarzer, P.G.Leiman. Phage Pierces the Host Cell Membrane with the Iron-Loaded Spike. Structure V. 20 326 2012.
ISSN: ISSN 0969-2126
PubMed: 22325780
DOI: 10.1016/J.STR.2011.12.009
Page generated: Sun Aug 4 18:15:45 2024

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