Arsenic in PDB 3llm: Crystal Structure Analysis of A Rna Helicase

The structure of Crystal Structure Analysis of A Rna Helicase, PDB code: 3llm was solved by P.Schutz, T.Karlberg, R.Collins, C.H.Arrowsmith, H.Berglund, C.Bountra, S.Flodin, A.Flores, S.Graslund, M.Hammarstrom, A.Johansson, I.Johansson, A.Kallas, P.Kraulis, T.Kotenyova, A.Kotzsch, N.Markova, M.Moche, T.K.Nielsen, P.Nordlund, T.Nyman, C.Persson, A.K.Roos, M.I.Siponen, L.Svensson, A.G.Thorsell, L.Tresaugues, S.Van Den Berg, E.Wahlberg, J.Weigelt, M.Welin, M.Wisniewska, H.M.Schuler, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	98.51 / 2.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	113.700, 113.700, 141.650, 90.00, 90.00, 120.00
R / Rfree (%)	21.1 / 23.8

The structure of Crystal Structure Analysis of A Rna Helicase also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Arsenic atom in the Crystal Structure Analysis of A Rna Helicase (pdb code 3llm). 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 A Rna Helicase, PDB code: 3llm:

Arsenic binding site 1 out of 1 in the Crystal Structure Analysis of A Rna Helicase


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 A Rna Helicase within 5.0Å range: probe atom residue distance (Å) B Occ A:As564 b:0.7 occ:1.00 AS A:CAC564 0.0 0.7 1.0 O1 A:CAC564 1.7 0.8 1.0 O2 A:CAC564 1.7 0.7 1.0 C1 A:CAC564 2.0 0.3 1.0 C2 A:CAC564 2.0 0.9 1.0 OD2 A:ASP377 4.2 98.8 1.0 OD1 A:ASP375 4.5 98.9 1.0 OD2 A:ASP375 4.6 98.2 1.0 CG A:ASP375 5.0 98.5 1.0

P.Schutz, E.Wahlberg, T.Karlberg, M.Hammarstrom, R.Collins, A.Flores, H.Schuler. Crystal Structure of Human Rna Helicase A (DHX9): Structural Basis For Unselective Nucleotide Base Binding in A Dead-Box Variant Protein. J.Mol.Biol. V. 400 768 2010.
ISSN: ISSN 0022-2836
PubMed: 20510246
DOI: 10.1016/J.JMB.2010.05.046