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Magnesium in PDB 1ido: I-Domain From Integrin CR3, MG2+ Bound

Protein crystallography data

The structure of I-Domain From Integrin CR3, MG2+ Bound, PDB code: 1ido was solved by J.-O.Lee, R.Liddington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.70
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 45.700, 45.700, 94.300, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the I-Domain From Integrin CR3, MG2+ Bound (pdb code 1ido). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the I-Domain From Integrin CR3, MG2+ Bound, PDB code: 1ido:

Magnesium binding site 1 out of 1 in 1ido

Go back to Magnesium Binding Sites List in 1ido
Magnesium binding site 1 out of 1 in the I-Domain From Integrin CR3, MG2+ Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of I-Domain From Integrin CR3, MG2+ Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:7.6
occ:1.00
O A:HOH404 2.0 5.6 1.0
O A:HOH403 2.0 2.7 1.0
OG1 A:THR209 2.1 6.0 1.0
OG A:SER142 2.2 7.8 1.0
OG A:SER144 2.2 6.2 1.0
CB A:SER142 3.2 5.2 1.0
CB A:SER144 3.3 4.1 1.0
CB A:THR209 3.3 4.2 1.0
CG2 A:THR209 3.6 2.0 1.0
O A:GLU244 4.0 5.9 1.0
N A:SER144 4.0 6.1 1.0
OD2 A:ASP242 4.1 4.5 1.0
OD1 A:ASP140 4.2 7.0 1.0
OD1 A:ASP242 4.2 6.3 1.0
CA A:SER144 4.2 7.2 1.0
OD2 A:ASP140 4.2 7.6 1.0
CA A:SER142 4.4 6.7 1.0
CA A:THR209 4.5 4.4 1.0
C A:SER142 4.5 9.9 1.0
CG A:ASP242 4.6 6.5 1.0
CG A:ASP140 4.7 7.0 1.0
N A:THR209 4.7 5.4 1.0
O A:SER142 4.8 11.6 1.0
N A:ILE145 4.8 8.2 1.0
C A:SER144 4.9 8.5 1.0
N A:GLY143 4.9 10.3 1.0
C A:ARG208 4.9 4.9 1.0
CG1 A:ILE145 5.0 6.7 1.0

Reference:

J.O.Lee, P.Rieu, M.A.Arnaout, R.Liddington. Crystal Structure of the A Domain From the Alpha Subunit of Integrin CR3 (CD11B/CD18). Cell(Cambridge,Mass.) V. 80 631 1995.
ISSN: ISSN 0092-8674
PubMed: 7867070
DOI: 10.1016/0092-8674(95)90517-0
Page generated: Tue Aug 13 04:58:01 2024

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