Arsenic in PDB 4ufc: Crystal Structure of the GH95 Enzyme BACOVA_03438

The structure of Crystal Structure of the GH95 Enzyme BACOVA_03438, PDB code: 4ufc was solved by A.Rogowski, J.A.Briggs, J.C.Mortimer, T.Tryfona, N.Terrapon, E.C.Lowe, A.Basle, C.Morland, A.M.Day, H.Zheng, T.E.Rogers, P.Thompson, A.R.Hawkins, M.P.Yadav, B.Henrissat, E.C.Martens, P.Dupree, H.J.Gilbert, D.N.Bolam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	134.93 / 2.81
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.692, 179.117, 205.181, 90.00, 90.00, 90.00
R / Rfree (%)	18.636 / 22.805

The structure of Crystal Structure of the GH95 Enzyme BACOVA_03438 also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Arsenic atom in the Crystal Structure of the GH95 Enzyme BACOVA_03438 (pdb code 4ufc). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of the GH95 Enzyme BACOVA_03438, PDB code: 4ufc:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Crystal Structure of the GH95 Enzyme BACOVA_03438


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of the GH95 Enzyme BACOVA_03438 within 5.0Å range: probe atom residue distance (Å) B Occ A:As1810 b:78.3 occ:1.00 AS A:CAC1810 0.0 78.3 1.0 O2 A:CAC1810 1.7 64.6 1.0 O1 A:CAC1810 1.8 58.6 1.0 C1 A:CAC1810 2.0 64.1 1.0 C2 A:CAC1810 2.0 65.4 1.0 OD2 A:ASP366 3.0 35.7 1.0 CG A:ASP366 3.8 35.0 1.0 OD1 A:ASP366 3.8 35.5 1.0 OE2 A:GLU210 4.1 44.4 1.0 O A:HIS109 4.1 35.7 1.0 OD1 A:ASP434 4.2 35.4 1.0 NZ A:LYS368 4.3 32.5 1.0 O A:GLY110 4.6 34.2 1.0 CB A:HIS109 4.6 36.8 1.0 OE1 A:GLU210 4.8 43.5 1.0 CD A:GLU210 4.8 43.7 1.0 C A:HIS109 4.9 35.9 1.0

Arsenic binding site 2 out of 2 in the Crystal Structure of the GH95 Enzyme BACOVA_03438


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of the GH95 Enzyme BACOVA_03438 within 5.0Å range: probe atom residue distance (Å) B Occ B:As1811 b:83.0 occ:1.00 AS B:CAC1811 0.0 83.0 1.0 O2 B:CAC1811 1.7 70.8 1.0 O1 B:CAC1811 1.7 67.4 1.0 C2 B:CAC1811 2.0 75.6 1.0 C1 B:CAC1811 2.0 77.3 1.0 OD2 B:ASP366 2.9 41.3 1.0 OD1 B:ASP366 3.6 41.1 1.0 CG B:ASP366 3.6 40.2 1.0 OE2 B:GLU210 4.2 48.4 1.0 O B:HIS109 4.3 41.6 1.0 OD1 B:ASP434 4.3 40.2 1.0 NZ B:LYS368 4.4 35.8 1.0 O B:GLY110 4.6 41.0 1.0 CB B:HIS109 4.8 42.1 1.0 OE1 B:GLU210 4.8 48.1 1.0 CD B:GLU210 4.8 48.3 1.0 C B:HIS109 5.0 41.8 1.0

A.Rogowski, J.A.Briggs, J.C.Mortimer, T.Tryfona, N.Terrapon, E.C.Lowe, A.Basle, C.Morland, A.M.Day, H.Zheng, T.E.Rogers, P.Thompson, A.R.Hawkins, M.P.Yadav, B.Henrissat, E.C.Martens, P.Dupree, H.J.Gilbert, D.N.Bolam. Glycan Complexity Dictates Microbial Resource Allocation in the Large Intestine. Nat.Commun. V. 6 7481 2015.
ISSN: ISSN 2041-1723
PubMed: 26112186
DOI: 10.1038/NCOMMS8481