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Calcium 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:

Magnesium (Mg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium 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:

Calcium binding site 1 out of 1 in 1d4x

Go back to Calcium Binding Sites List in 1d4x
Calcium 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 Calcium with other atoms in the Ca 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
G:Ca681

b:9.6
occ:0.15
O G:VAL121 2.1 26.1 1.0
O G:GLY41 2.1 16.4 1.0
OE2 G:GLU73 2.4 22.9 1.0
O G:HOH864 2.5 34.1 1.0
OD2 G:ASP42 2.6 25.3 1.0
OE1 G:GLU73 2.6 20.5 1.0
CD G:GLU73 2.8 17.4 1.0
O G:HOH932 2.9 50.8 1.0
C G:GLY41 3.2 16.4 1.0
C G:VAL121 3.3 29.2 1.0
N G:VAL121 3.8 25.0 1.0
CG G:ASP42 3.8 25.4 1.0
CA G:ASP42 3.9 13.3 1.0
N G:ASP42 4.0 14.9 1.0
CG2 G:VAL121 4.0 34.4 1.0
CA G:VAL121 4.1 29.1 1.0
CA G:GLY41 4.2 17.2 1.0
N G:ALA122 4.3 30.4 1.0
CG G:GLU73 4.3 13.1 1.0
O G:HOH714 4.3 15.1 1.0
C G:GLY120 4.4 24.4 1.0
CB G:ASP42 4.5 14.8 1.0
C G:ALA122 4.5 29.4 1.0
CA G:ALA122 4.5 31.8 1.0
CA G:CYS69 4.7 12.9 1.0
CB G:VAL121 4.7 29.8 1.0
N G:SER123 4.7 29.2 1.0
O G:ALA122 4.7 28.7 1.0
OD1 G:ASP42 4.7 25.5 1.0
CA G:GLY120 4.8 25.0 1.0
N G:SER70 4.9 15.1 1.0
O G:HOH764 4.9 23.7 1.0
O G:HOH1087 5.0 48.5 1.0
CB G:CYS69 5.0 11.9 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: Thu Jul 11 07:23:16 2024

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