Calcium in PDB 1c1y: Crystal Structure of Rap.Gmppnp in Complex with the Ras- Binding-Domain of C-RAF1 Kinase (Rafrbd).

The structure of Crystal Structure of Rap.Gmppnp in Complex with the Ras- Binding-Domain of C-RAF1 Kinase (Rafrbd)., PDB code: 1c1y was solved by N.Nassar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.170, 71.880, 100.200, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 25.7

The structure of Crystal Structure of Rap.Gmppnp in Complex with the Ras- Binding-Domain of C-RAF1 Kinase (Rafrbd). also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Calcium atom in the Crystal Structure of Rap.Gmppnp in Complex with the Ras- Binding-Domain of C-RAF1 Kinase (Rafrbd). (pdb code 1c1y). 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 Rap.Gmppnp in Complex with the Ras- Binding-Domain of C-RAF1 Kinase (Rafrbd)., PDB code: 1c1y:

Calcium binding site 1 out of 1 in the Crystal Structure of Rap.Gmppnp in Complex with the Ras- Binding-Domain of C-RAF1 Kinase (Rafrbd).


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 Rap.Gmppnp in Complex with the Ras- Binding-Domain of C-RAF1 Kinase (Rafrbd). within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca173 b:27.3 occ:1.00 O B:GLY123 2.4 28.9 1.0 O B:HOH413 2.4 28.2 1.0 OE2 B:GLU125 2.5 23.9 1.0 O B:HOH420 2.6 31.5 1.0 OE1 B:GLU125 2.6 28.1 1.0 CD B:GLU125 2.9 26.6 1.0 C B:GLY123 3.6 29.6 1.0 NE2 B:HIS103 4.2 30.1 1.0 CD2 B:HIS103 4.2 30.9 1.0 CA B:GLU124 4.3 27.1 1.0 N B:GLU124 4.4 27.6 1.0 CG B:GLU125 4.4 25.1 1.0 C B:GLU124 4.6 26.4 1.0 CA B:GLY123 4.6 29.8 1.0 N B:GLU125 4.6 24.5 1.0 O B:HOH417 4.7 25.8 1.0 O B:HOH450 4.7 36.3 1.0 O B:HOH481 4.8 47.0 1.0

N.Nassar, N.Nassar. N/A N/A.
ISSN: ISSN 0028-0836
PubMed: 7791872
DOI: 10.1038/375554A0