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Arsenic in PDB 5ed4: Structure of A Phop-Dna Complex

Enzymatic activity of Structure of A Phop-Dna Complex

All present enzymatic activity of Structure of A Phop-Dna Complex:
3.1.3.1;

Protein crystallography data

The structure of Structure of A Phop-Dna Complex, PDB code: 5ed4 was solved by S.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.60 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 92.240, 98.176, 167.888, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 22.7

Other elements in 5ed4:

The structure of Structure of A Phop-Dna Complex also contains other interesting chemical elements:

Calcium (Ca) 6 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Structure of A Phop-Dna Complex (pdb code 5ed4). 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 Structure of A Phop-Dna Complex, PDB code: 5ed4:

Arsenic binding site 1 out of 1 in 5ed4

Go back to Arsenic Binding Sites List in 5ed4
Arsenic binding site 1 out of 1 in the Structure of A Phop-Dna Complex


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structure of A Phop-Dna Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
E:As303

b:0.2
occ:1.00
AS E:CAC303 0.0 0.2 1.0
O2 E:CAC303 1.7 0.4 1.0
O1 E:CAC303 1.7 0.2 1.0
C1 E:CAC303 2.0 0.6 1.0
C2 E:CAC303 2.0 0.3 1.0
OE1 E:GLU157 4.1 92.1 1.0
CG E:TRP166 4.2 67.1 1.0
O E:HOH432 4.3 78.3 1.0
CD1 E:TRP166 4.3 72.2 1.0
CD2 E:TRP166 4.3 67.8 1.0
NE1 E:TRP166 4.5 74.8 1.0
CE2 E:TRP166 4.5 75.6 1.0
CD E:GLU157 4.5 88.2 1.0
CB E:TRP166 4.7 63.0 1.0
CA E:GLY169 4.8 73.8 1.0
CE3 E:TRP166 4.8 68.5 1.0
OE2 E:GLU157 4.9 88.2 1.0
O E:GLY169 5.0 80.4 1.0

Reference:

X.He, L.Wang, S.Wang. Structural Basis of Dna Sequence Recognition By the Response Regulator Phop in Mycobacterium Tuberculosis. Sci Rep V. 6 24442 2016.
ISSN: ESSN 2045-2322
PubMed: 27079268
DOI: 10.1038/SREP24442
Page generated: Sat Dec 12 01:46:36 2020

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