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Zinc in PDB 3zyq: Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution

Protein crystallography data

The structure of Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution, PDB code: 3zyq was solved by J.R.C.Muniz, V.Ayinampudi, L.Shrestha, T.Krojer, M.Vollmar, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, A.Bullock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 85.27 / 1.48
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 38.256, 34.346, 170.533, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 21.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution (pdb code 3zyq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution, PDB code: 3zyq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3zyq

Go back to Zinc Binding Sites List in 3zyq
Zinc binding site 1 out of 2 in the Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1222

b:16.6
occ:1.00
SG A:CYS193 2.3 18.2 1.0
SG A:CYS190 2.3 16.7 1.0
SG A:CYS169 2.3 18.4 1.0
SG A:CYS166 2.4 13.7 1.0
CB A:CYS193 3.2 17.4 1.0
CB A:CYS166 3.3 13.3 1.0
CB A:CYS169 3.3 19.0 1.0
CB A:CYS190 3.5 14.7 1.0
N A:CYS169 3.8 17.2 1.0
N A:CYS190 4.0 12.8 1.0
CA A:CYS169 4.1 17.0 1.0
N A:CYS193 4.2 16.2 1.0
CG1 A:VAL171 4.2 19.6 1.0
CA A:CYS190 4.2 12.6 1.0
CA A:CYS193 4.3 16.9 1.0
O A:HOH2128 4.6 39.1 1.0
CA A:CYS166 4.7 12.5 1.0
CB A:ARG168 4.7 16.9 1.0
C A:CYS190 4.8 13.8 1.0
O A:CYS190 4.8 14.2 1.0
C A:CYS169 4.8 16.7 1.0
C A:ARG168 4.9 16.5 1.0
N A:ARG170 4.9 17.3 1.0

Zinc binding site 2 out of 2 in 3zyq

Go back to Zinc Binding Sites List in 3zyq
Zinc binding site 2 out of 2 in the Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1223

b:15.7
occ:1.00
SG A:CYS182 2.3 14.3 1.0
SG A:CYS215 2.3 17.9 1.0
SG A:CYS185 2.4 15.8 1.0
SG A:CYS212 2.4 16.8 1.0
CB A:CYS182 3.2 12.3 1.0
CB A:CYS185 3.2 15.4 1.0
CB A:CYS215 3.2 16.0 1.0
CB A:CYS212 3.6 15.6 1.0
N A:CYS185 3.7 13.6 1.0
N A:CYS212 3.9 13.0 1.0
CA A:CYS185 4.1 14.8 1.0
CA A:CYS212 4.3 14.8 1.0
CA A:CYS215 4.4 16.6 1.0
N A:CYS215 4.5 15.6 1.0
CB A:ALA184 4.5 13.9 1.0
O A:HOH2152 4.5 34.3 1.0
CA A:CYS182 4.6 10.2 1.0
CE2 A:PHE189 4.6 14.4 1.0
C A:ALA184 4.6 15.5 1.0
CZ A:PHE189 4.8 15.6 1.0
C A:CYS212 4.9 14.0 1.0
CA A:ALA184 4.9 13.4 1.0
N A:ALA184 4.9 12.6 1.0
C A:CYS185 4.9 14.3 1.0
O A:CYS212 5.0 15.7 1.0

Reference:

J.R.C.Muniz, V.Ayinampudi, L.Shrestha, T.Krojer, M.Vollmar, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, A.Bullock. Crystal Structure of the Tandem Vhs and Fyve Domains of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) at 1.48 A Resolution To Be Published.
Page generated: Sat Oct 26 18:44:58 2024

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