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Magnesium in PDB 1d4x: Crystal Structure of Caenorhabditis Elegans Mg-Atp Actin Complexed with Human Gelsolin Segment 1 at 1.75 A Resolution.

Protein crystallography data

The structure of Crystal Structure of Caenorhabditis Elegans Mg-Atp Actin Complexed with Human Gelsolin Segment 1 at 1.75 A Resolution., PDB code: 1d4x was solved by S.Vorobiev, S.Ono, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.20 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 177.820, 68.989, 56.593, 90.00, 104.15, 90.00
R / Rfree (%) 19.9 / 23.3

Other elements in 1d4x:

The structure of Crystal Structure of Caenorhabditis Elegans Mg-Atp Actin Complexed with Human Gelsolin Segment 1 at 1.75 A Resolution. also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Caenorhabditis Elegans Mg-Atp Actin Complexed with Human Gelsolin Segment 1 at 1.75 A Resolution. (pdb code 1d4x). 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 Crystal Structure of Caenorhabditis Elegans Mg-Atp Actin Complexed with Human Gelsolin Segment 1 at 1.75 A Resolution., PDB code: 1d4x:

Magnesium binding site 1 out of 1 in 1d4x

Go back to Magnesium Binding Sites List in 1d4x
Magnesium binding site 1 out of 1 in the Crystal Structure of Caenorhabditis Elegans Mg-Atp Actin Complexed with Human Gelsolin Segment 1 at 1.75 A Resolution.


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 Caenorhabditis Elegans Mg-Atp Actin Complexed with Human Gelsolin Segment 1 at 1.75 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg680

b:19.0
occ:1.00
O A:HOH701 2.2 11.8 1.0
O1G A:ATP676 2.2 17.7 1.0
O A:HOH716 2.2 13.8 1.0
O A:HOH713 2.2 15.8 1.0
O A:HOH704 2.3 13.0 1.0
O1B A:ATP676 2.4 15.0 1.0
PG A:ATP676 3.3 15.7 1.0
PB A:ATP676 3.4 12.7 1.0
O3B A:ATP676 3.5 15.3 1.0
O3G A:ATP676 3.8 13.9 1.0
O A:HOH792 3.9 29.2 1.0
O3A A:ATP676 4.0 11.3 1.0
O A:HOH775 4.0 24.2 1.0
O A:HOH712 4.1 16.9 1.0
O1A A:ATP676 4.1 13.3 1.0
OE1 A:GLN137 4.2 12.3 1.0
OD1 A:ASP11 4.3 14.0 1.0
NZ A:LYS18 4.3 12.1 1.0
OD1 A:ASP154 4.4 31.4 1.0
O A:HOH805 4.4 26.2 1.0
OD2 A:ASP11 4.5 14.1 1.0
CA A:GLY13 4.5 14.4 1.0
O A:HOH849 4.5 27.4 1.0
O2B A:ATP676 4.5 15.7 1.0
PA A:ATP676 4.6 13.5 1.0
OD2 A:ASP154 4.6 26.1 1.0
CD A:GLN137 4.6 11.2 1.0
O2G A:ATP676 4.6 15.5 1.0
CG A:ASP11 4.8 11.2 1.0
CG A:ASP154 4.9 26.4 1.0
O2A A:ATP676 5.0 13.4 1.0

Reference:

S.Vorobiev, B.Strokopytov, D.G.Drubin, C.Frieden, S.Ono, J.Condeelis, P.A.Rubenstein, S.C.Almo. The Structure of Nonvertebrate Actin: Implications For the Atp Hydrolytic Mechanism. Proc.Natl.Acad.Sci.Usa V. 100 5760 2003.
ISSN: ISSN 0027-8424
PubMed: 12732734
DOI: 10.1073/PNAS.0832273100
Page generated: Mon Dec 14 05:50:00 2020

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