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Calcium in PDB 3vrp: Crystal Structure of the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide

Enzymatic activity of Crystal Structure of the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide

All present enzymatic activity of Crystal Structure of the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide, PDB code: 3vrp was solved by K.Takeshita, T.Tezuka, Y.Isozaki, E.Yamashita, M.Suzuki, Y.Yamanashi, T.Yamamoto, A.Nakagawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.78 / 1.52
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 93.357, 108.710, 54.936, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide (pdb code 3vrp). 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 the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide, PDB code: 3vrp:

Calcium binding site 1 out of 1 in 3vrp

Go back to Calcium Binding Sites List in 3vrp
Calcium binding site 1 out of 1 in the Crystal Structure of the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide


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 the Tyrosine Kinase Binding Domain of Cbl-C in Complex with Phospho-Egfr Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:10.9
occ:0.65
 OD1 A:ASP199 2.3 8.4 1.0
O A:HIS205 2.3 9.0 1.0
OE2 A:GLU210 2.4 10.4 1.0
O A:HOH536 2.5 12.4 1.0
OG1 A:THR201 2.6 7.8 1.0
OG A:SER203 2.6 8.3 1.0
OE1 A:GLU210 2.7 13.1 1.0
CD A:GLU210 2.9 12.7 1.0
CG A:ASP199 3.4 8.4 1.0
C A:HIS205 3.5 7.3 1.0
CB A:SER203 3.7 8.7 1.0
CB A:THR201 3.9 6.9 1.0
O A:HOH550 3.9 12.0 1.0
N A:SER203 4.0 6.9 1.0
N A:THR201 4.0 6.4 1.0
N A:HIS205 4.1 7.7 1.0
O A:HOH507 4.1 10.4 1.0
OD2 A:ASP199 4.2 10.5 1.0
CA A:ASP199 4.3 7.3 1.0
CA A:SER203 4.3 7.3 1.0
CA A:THR201 4.3 7.3 1.0
N A:CYS202 4.4 7.5 1.0
CA A:HIS205 4.4 6.9 1.0
CB A:ASP199 4.4 8.2 1.0
CG A:GLU210 4.4 7.8 1.0
CG2 A:THR201 4.5 7.1 1.0
N A:VAL206 4.5 6.1 1.0
C A:ASP199 4.5 8.0 1.0
C A:THR201 4.5 7.3 1.0
OE2 A:GLU134 4.5 9.4 1.0
N A:LEU200 4.5 7.6 1.0
CA A:VAL206 4.6 5.9 1.0
N A:GLY204 4.6 7.1 1.0
C A:SER203 4.8 7.6 1.0
CB A:HIS205 4.8 8.9 1.0
N A:SER207 4.9 5.0 1.0

Reference:

K.Takeshita, T.Tezuka, Y.Isozaki, E.Yamashita, M.Suzuki, M.Kim, Y.Yamanashi, T.Yamamoto, A.Nakagawa. Structural Flexibility Regulates Phosphopeptide-Binding Activity of the Tyrosine Kinase Binding Domain of Cbl-C. J.Biochem. V. 152 487 2012.
ISSN: ISSN 0021-924X
PubMed: 22888118
DOI: 10.1093/JB/MVS085
Page generated: Tue Jul 8 17:40:43 2025

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