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Arsenic in PDB 4j5g: Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant

Enzymatic activity of Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant

All present enzymatic activity of Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant:
3.1.27.3;

Protein crystallography data

The structure of Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant, PDB code: 4j5g was solved by L.Urbanikova, J.Sevcik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.71 / 1.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.125, 64.196, 78.233, 90.00, 90.00, 90.00
R / Rfree (%) 11.2 / 15

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant (pdb code 4j5g). 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 Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant, PDB code: 4j5g:

Arsenic binding site 1 out of 1 in 4j5g

Go back to Arsenic Binding Sites List in 4j5g
Arsenic binding site 1 out of 1 in the Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure Analysis of Streptomyces Aureofaciens Ribonuclease Sa T95A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As102

b:38.6
occ:0.50
AS B:CAC102 0.0 38.6 0.5
O1 B:CAC102 1.7 24.7 0.5
O2 B:CAC102 1.7 22.7 0.5
C1 B:CAC102 1.9 21.2 0.5
C2 B:CAC102 2.0 34.5 0.5
O B:HOH252 3.5 15.9 1.0
O B:HOH299 3.7 22.7 1.0
N B:GLN77 3.8 12.1 1.0
O B:HOH270 3.8 18.5 1.0
O B:HOH379 3.9 45.6 1.0
O B:HOH350 4.0 29.7 1.0
CA B:GLN77 4.5 12.1 1.0
CG B:GLN77 4.6 16.3 1.0
O B:HOH251 4.6 15.3 1.0
O B:HOH248 4.6 15.0 1.0
CA B:THR76 4.6 15.3 1.0
C B:THR76 4.7 11.9 1.0
CG2 B:THR76 4.9 27.8 1.0

Reference:

C.N.Pace, H.Fu, K.Lee Fryar, J.Landua, S.R.Trevino, D.Schell, R.L.Thurlkill, S.Imura, J.M.Scholtz, K.Gajiwala, J.Sevcik, L.Urbanikova, J.K.Myers, K.Takano, E.J.Hebert, B.A.Shirley, G.R.Grimsley. Contribution of Hydrogen Bonds to Protein Stability. Protein Sci. V. 23 652 2014.
ISSN: ISSN 0961-8368
PubMed: 24591301
DOI: 10.1002/PRO.2449
Page generated: Wed Jul 10 12:11:41 2024

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