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Iodine in PDB 3usm: Crystal Structure of Leut Bound to L-Selenomethionine in Space Group C2 From Lipid Bicelles (Collected at 1.2 A)

Protein crystallography data

The structure of Crystal Structure of Leut Bound to L-Selenomethionine in Space Group C2 From Lipid Bicelles (Collected at 1.2 A), PDB code: 3usm was solved by H.Wang, J.Elferich, E.Gouaux, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.48 / 3.01
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.254, 90.396, 82.164, 90.00, 103.62, 90.00
R / Rfree (%) 20.8 / 21.9

Other elements in 3usm:

The structure of Crystal Structure of Leut Bound to L-Selenomethionine in Space Group C2 From Lipid Bicelles (Collected at 1.2 A) also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Iodine Binding Sites:

The binding sites of Iodine atom in the Crystal Structure of Leut Bound to L-Selenomethionine in Space Group C2 From Lipid Bicelles (Collected at 1.2 A) (pdb code 3usm). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total only one binding site of Iodine was determined in the Crystal Structure of Leut Bound to L-Selenomethionine in Space Group C2 From Lipid Bicelles (Collected at 1.2 A), PDB code: 3usm:

Iodine binding site 1 out of 1 in 3usm

Go back to Iodine Binding Sites List in 3usm
Iodine binding site 1 out of 1 in the Crystal Structure of Leut Bound to L-Selenomethionine in Space Group C2 From Lipid Bicelles (Collected at 1.2 A)


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structure of Leut Bound to L-Selenomethionine in Space Group C2 From Lipid Bicelles (Collected at 1.2 A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I521

b:90.1
occ:0.50
OE1 A:GLU370 3.8 93.1 1.0
CD A:GLU370 4.2 84.0 1.0
CG A:GLU370 4.2 80.4 1.0
CB A:PRO78 4.3 74.3 1.0
N A:ALA79 4.3 63.0 1.0
CB A:ALA504 4.3 73.4 1.0
CG1 A:VAL501 4.3 71.7 1.0
CB A:ALA79 4.4 65.2 1.0
CA A:ALA79 4.4 65.9 1.0
C A:PRO78 4.5 69.5 1.0
CE1 A:PHE366 4.5 76.1 1.0
CB A:GLU370 4.6 68.9 1.0
O A:VAL501 4.6 72.9 1.0
O A:PRO78 4.8 71.4 1.0
N A:GLU505 4.9 90.2 1.0

Reference:

H.Wang, J.Elferich, E.Gouaux. Structures of Leut in Bicelles Define Conformation and Substrate Binding in A Membrane-Like Context. Nat.Struct.Mol.Biol. V. 19 212 2012.
ISSN: ISSN 1545-9993
PubMed: 22245965
DOI: 10.1038/NSMB.2215
Page generated: Sun Aug 11 16:59:46 2024

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