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Magnesium in PDB 3dlh: Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex

Protein crystallography data

The structure of Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex, PDB code: 3dlh was solved by Y.Wang, G.Sheng, D.J.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 3.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.744, 114.629, 175.689, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 28.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex (pdb code 3dlh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex, PDB code: 3dlh:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 3dlh

Go back to Magnesium Binding Sites List in 3dlh
Magnesium binding site 1 out of 3 in the Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg686

b:31.0
occ:1.00
OP1 X:DA3 2.1 45.3 1.0
OP1 X:DT1 2.3 64.8 1.0
OXT A:VAL685 2.5 45.1 1.0
O A:VAL685 2.7 43.3 1.0
C A:VAL685 2.9 42.3 1.0
P X:DA3 3.3 49.2 1.0
NZ A:LYS457 3.5 35.0 1.0
OE1 A:GLN433 3.5 47.8 1.0
P X:DT1 3.6 65.1 1.0
O3' X:DG2 3.6 50.4 1.0
O5' X:DT1 3.8 64.0 1.0
NE2 A:GLN433 4.1 49.0 1.0
OP3 X:DT1 4.2 66.7 1.0
OP2 X:DA3 4.2 49.4 1.0
CD A:GLN433 4.3 47.5 1.0
CA A:VAL685 4.4 40.3 1.0
C5' X:DT1 4.4 64.7 1.0
O5' X:DA3 4.5 47.9 1.0
CG2 A:VAL685 4.7 38.9 1.0
C5' X:DA3 4.7 45.5 1.0
CE A:LYS457 4.8 37.7 1.0
OP2 X:DT1 4.8 64.7 1.0
CB A:VAL685 4.8 38.6 1.0
C3' X:DG2 4.8 49.8 1.0

Magnesium binding site 2 out of 3 in 3dlh

Go back to Magnesium Binding Sites List in 3dlh
Magnesium binding site 2 out of 3 in the Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg687

b:57.9
occ:1.00
O A:GLY459 2.8 58.2 1.0
OE1 A:GLN342 2.9 94.1 1.0
NE2 A:GLN342 3.3 93.9 1.0
CD A:GLN342 3.5 93.8 1.0
CB A:GLU680 3.7 53.5 1.0
C A:GLY459 3.8 58.4 1.0
CG A:GLU680 4.0 57.1 1.0
O A:HOH702 4.0 37.4 1.0
CA A:GLY459 4.1 56.2 1.0
OD2 A:ASP678 4.3 62.9 1.0
OE1 A:GLU680 4.3 60.0 1.0
CD A:GLU680 4.7 59.8 1.0
O A:ALA458 4.8 52.8 1.0
CG A:GLN342 5.0 92.5 1.0

Magnesium binding site 3 out of 3 in 3dlh

Go back to Magnesium Binding Sites List in 3dlh
Magnesium binding site 3 out of 3 in the Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Guide-Strand-Containing Argonaute Protein Silencing Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
Y:Mg2

b:26.8
occ:1.00
OP1 Y:DA103 2.1 58.4 1.0
OXT B:VAL685 2.3 53.1 1.0
OP2 Y:DT101 2.4 59.2 1.0
O B:VAL685 2.6 53.2 1.0
C B:VAL685 2.8 53.1 1.0
OP3 Y:DT101 3.2 58.3 1.0
P Y:DT101 3.3 58.3 1.0
P Y:DA103 3.4 59.3 1.0
OP2 Y:DA103 4.0 60.4 1.0
O5' Y:DT101 4.0 59.1 1.0
NZ B:LYS457 4.0 52.3 1.0
CA B:VAL685 4.3 52.1 1.0
O5' Y:DA103 4.3 58.2 1.0
O3' Y:DG102 4.4 59.9 1.0
OE1 B:GLN433 4.4 48.7 1.0
OP1 Y:DT101 4.6 59.3 1.0
C5' Y:DT101 4.9 61.3 1.0
CE B:LYS457 4.9 50.7 1.0

Reference:

Y.Wang, G.Sheng, S.Juranek, T.Tuschl, D.J.Patel. Structure of the Guide-Strand-Containing Argonaute Silencing Complex. Nature V. 456 209 2008.
ISSN: ISSN 0028-0836
PubMed: 18754009
DOI: 10.1038/NATURE07315
Page generated: Sun Aug 10 20:08:40 2025

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