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Arsenic in PDB 3gh3: Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.

Enzymatic activity of Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.

All present enzymatic activity of Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.:
3.2.2.5;

Protein crystallography data

The structure of Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex., PDB code: 3gh3 was solved by P.F.Egea, H.Muller-Steffner, R.M.Stroud, E.Kellenberger, N.Oppenheimer, F.Schuber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.44 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.483, 80.879, 151.790, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 22.3

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex. (pdb code 3gh3). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex., PDB code: 3gh3:

Arsenic binding site 1 out of 1 in 3gh3

Go back to Arsenic Binding Sites List in 3gh3
Arsenic binding site 1 out of 1 in the Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As1001

b:86.7
occ:1.00
AS B:CAC1001 0.0 86.7 1.0
O1 B:CAC1001 1.7 48.6 1.0
O2 B:CAC1001 1.7 65.5 1.0
C2 B:CAC1001 2.0 0.5 1.0
C1 B:CAC1001 2.0 79.4 1.0
O B:HOH19 3.6 24.1 1.0
O B:HOH309 3.7 22.3 1.0
O B:HOH515 3.9 47.3 1.0
O B:HOH483 4.0 40.3 1.0
N B:ILE213 4.1 18.8 1.0
O B:HOH410 4.1 39.1 1.0
CB B:SER212 4.1 18.9 1.0
CE B:LYS120 4.2 63.9 1.0
O B:HOH416 4.3 46.2 1.0
CA B:SER212 4.4 23.1 1.0
CG1 B:ILE213 4.6 46.7 1.0
C B:SER212 4.8 18.3 1.0
CB B:ILE213 4.9 23.3 1.0

Reference:

P.F.Egea, H.Muller-Steffner, I.Kuhn, C.Cakir-Kiefer, N.J.Oppenheimer, R.M.Stroud, E.Kellenberger, F.Schuber. Insights Into the Mechanism of Bovine CD38/Nad+Glycohydrolase From the X-Ray Structures of Its Michaelis Complex and Covalently-Trapped Intermediates. Plos One V. 7 34918 2012.
ISSN: ESSN 1932-6203
PubMed: 22529956
DOI: 10.1371/JOURNAL.PONE.0034918
Page generated: Tue Oct 27 16:50:19 2020

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