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Calcium in PDB 2y1n: Structure of C-Cbl-Zap-70 Peptide Complex

Enzymatic activity of Structure of C-Cbl-Zap-70 Peptide Complex

All present enzymatic activity of Structure of C-Cbl-Zap-70 Peptide Complex:
2.7.10.2;

Protein crystallography data

The structure of Structure of C-Cbl-Zap-70 Peptide Complex, PDB code: 2y1n was solved by H.Dou, G.J.Sibbet, D.T.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.423 / 2.00
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 93.570, 93.570, 189.599, 90.00, 90.00, 120.00
R / Rfree (%) 15.82 / 18.04

Other elements in 2y1n:

The structure of Structure of C-Cbl-Zap-70 Peptide Complex also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of C-Cbl-Zap-70 Peptide Complex (pdb code 2y1n). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of C-Cbl-Zap-70 Peptide Complex, PDB code: 2y1n:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2y1n

Go back to Calcium Binding Sites List in 2y1n
Calcium binding site 1 out of 2 in the Structure of C-Cbl-Zap-70 Peptide Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of C-Cbl-Zap-70 Peptide Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1438

b:40.6
occ:1.00
O A:TYR235 2.4 31.9 1.0
OD1 A:ASN233 2.5 31.4 1.0
OG1 A:THR231 2.6 33.1 1.0
OE2 A:GLU240 2.7 28.4 1.0
OD1 A:ASP229 2.7 28.4 1.0
O A:HOH2071 2.7 28.7 1.0
OE1 A:GLU240 2.8 24.2 1.0
CD A:GLU240 3.1 26.8 1.0
C A:TYR235 3.5 31.6 1.0
CG A:ASN233 3.6 30.4 1.0
CG A:ASP229 3.7 28.2 1.0
CB A:THR231 3.9 28.4 1.0
N A:THR231 4.0 27.4 1.0
N A:TYR235 4.1 31.1 1.0
N A:ASN233 4.1 31.5 1.0
CA A:TYR235 4.2 31.3 1.0
O A:HOH2105 4.2 35.8 1.0
N A:CYS232 4.3 28.0 1.0
CA A:THR231 4.3 27.9 1.0
OD2 A:ASP229 4.4 34.0 1.0
CB A:TYR235 4.4 31.8 1.0
ND2 A:ASN233 4.4 29.4 1.0
N A:ILE236 4.4 29.9 1.0
CA A:ASP229 4.4 26.2 1.0
CG2 A:THR231 4.5 27.9 1.0
C A:THR231 4.5 28.0 1.0
CA A:ILE236 4.5 28.4 1.0
CG A:GLU240 4.5 24.7 1.0
C A:ASP229 4.6 29.1 1.0
CB A:ASP229 4.6 27.2 1.0
CB A:ASN233 4.6 33.4 1.0
N A:LEU230 4.7 28.5 1.0
CA A:ASN233 4.7 30.8 1.0
N A:ASP234 4.8 31.3 1.0
N A:SER237 4.9 31.5 1.0
C A:ASN233 4.9 30.0 1.0
OE2 A:GLU164 4.9 30.6 1.0
O A:HOH2072 4.9 32.5 1.0
CD1 A:ILE236 5.0 27.5 1.0
O A:ASP229 5.0 26.0 1.0

Calcium binding site 2 out of 2 in 2y1n

Go back to Calcium Binding Sites List in 2y1n
Calcium binding site 2 out of 2 in the Structure of C-Cbl-Zap-70 Peptide Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of C-Cbl-Zap-70 Peptide Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca1438

b:39.5
occ:1.00
OD1 C:ASN233 2.5 33.3 1.0
O C:TYR235 2.5 30.5 1.0
OG1 C:THR231 2.5 27.0 1.0
OD1 C:ASP229 2.6 28.5 1.0
OE1 C:GLU240 2.7 28.1 1.0
OE2 C:GLU240 2.8 28.4 1.0
O C:HOH2080 3.0 30.6 1.0
CD C:GLU240 3.1 29.5 1.0
CG C:ASP229 3.4 30.1 1.0
C C:TYR235 3.6 31.2 1.0
CG C:ASN233 3.6 32.6 1.0
CB C:THR231 3.8 25.4 1.0
N C:THR231 3.9 22.9 1.0
OD2 C:ASP229 3.9 31.7 1.0
N C:ASN233 4.1 28.0 1.0
CA C:ASP229 4.1 27.5 1.0
N C:TYR235 4.1 35.3 1.0
N C:CYS232 4.1 28.0 1.0
CA C:THR231 4.2 24.7 1.0
CB C:ASP229 4.3 27.6 1.0
ND2 C:ASN233 4.3 28.1 1.0
C C:ASP229 4.3 31.0 1.0
C C:THR231 4.3 28.6 1.0
CA C:TYR235 4.4 35.2 1.0
N C:LEU230 4.5 28.0 1.0
CG2 C:THR231 4.5 26.0 1.0
CA C:ILE236 4.5 31.2 1.0
N C:ILE236 4.5 32.8 1.0
CB C:TYR235 4.6 37.8 1.0
CG C:GLU240 4.6 28.3 1.0
CB C:ASN233 4.7 31.9 1.0
N C:ASP234 4.7 31.9 1.0
CD1 C:ILE236 4.7 29.2 1.0
CA C:ASN233 4.7 31.9 1.0
C C:ASN233 4.9 32.9 1.0
O C:ASP229 4.9 29.5 1.0
CA C:CYS232 5.0 29.0 1.0

Reference:

H.Dou, L.Buetow, A.Hock, G.J.Sibbet, K.H.Vousden, D.T.Huang. Structural Basis For Autoinhibition and Phosphorylation- Dependent Activation of C-Cbl. Nat.Struct.Mol.Biol. V. 19 184 2012.
ISSN: ISSN 1545-9993
PubMed: 22266821
DOI: 10.1038/NSMB.2231
Page generated: Fri Jul 12 19:18:41 2024

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