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Calcium in PDB 4a4b: Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex

Enzymatic activity of Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex

All present enzymatic activity of Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex:
2.7.10.2; 6.3.2.19;

Protein crystallography data

The structure of Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex, PDB code: 4a4b was solved by H.Dou, L.Buetow, A.Hock, G.J.Sibbet, K.H.Vousden, D.T.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.725 / 2.79
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.112, 74.112, 449.706, 90.00, 90.00, 120.00
R / Rfree (%) 18.74 / 26.68

Other elements in 4a4b:

The structure of Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex (pdb code 4a4b). 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 Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex, PDB code: 4a4b:

Calcium binding site 1 out of 1 in 4a4b

Go back to Calcium Binding Sites List in 4a4b
Calcium binding site 1 out of 1 in the Structure of Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 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 Modified PHOSPHOTYR371-C-Cbl-UBCH5B-Zap-70 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1438

b:0.5
occ:1.00
OD1 A:ASN233 2.4 78.6 1.0
OD1 A:ASP229 2.4 65.2 1.0
OE2 A:GLU240 2.6 70.9 1.0
O A:TYR235 2.6 65.2 1.0
OE1 A:GLU240 2.8 78.1 1.0
OG1 A:THR231 2.8 65.0 1.0
CD A:GLU240 3.0 73.5 1.0
CG A:ASP229 3.2 60.9 1.0
CG A:ASN233 3.5 78.2 1.0
C A:TYR235 3.6 58.5 1.0
N A:ASN233 3.9 64.0 1.0
CA A:ASP229 3.9 52.6 1.0
OD2 A:ASP229 4.0 60.7 1.0
N A:THR231 4.0 48.6 1.0
CB A:ASP229 4.0 51.8 1.0
N A:CYS232 4.1 45.0 1.0
CB A:THR231 4.1 56.6 1.0
N A:TYR235 4.2 60.7 1.0
N A:LEU230 4.2 50.0 1.0
C A:ASP229 4.2 59.3 1.0
ND2 A:ASN233 4.2 85.2 1.0
CA A:THR231 4.3 53.8 1.0
CA A:TYR235 4.4 58.9 1.0
C A:THR231 4.4 51.2 1.0
N A:ILE236 4.5 58.9 1.0
CG A:GLU240 4.5 67.2 1.0
CA A:ASN233 4.5 66.0 1.0
CB A:ASN233 4.5 72.8 1.0
N A:ASP234 4.6 58.0 1.0
CA A:ILE236 4.6 51.7 1.0
CB A:TYR235 4.7 58.8 1.0
C A:ASN233 4.8 68.2 1.0
CA A:CYS232 4.8 52.1 1.0
C A:CYS232 4.8 59.0 1.0
O A:ASP229 4.9 63.5 1.0
N A:SER237 5.0 51.8 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: Sat Dec 12 04:38:06 2020

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