Arsenic in PDB 5d8q: 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa

All present enzymatic activity of 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa:
1.16.3.1;

The structure of 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa, PDB code: 5d8q was solved by S.Lovell, K.P.Battaile, Y.Wang, H.Yao, M.Rivera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.43 / 2.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	117.864, 169.989, 125.662, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 26.3

The structure of 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Magnesium	(Mg)	12 atoms
Iron	(Fe)	7 atoms

The binding sites of Arsenic atom in the 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa (pdb code 5d8q). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 3 binding sites of Arsenic where determined in the 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa, PDB code: 5d8q:
Jump to Arsenic binding site number: 1; 2; 3;

Arsenic binding site 1 out of 3 in the 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:As201 b:20.7 occ:1.00 OD1 K:ASN148 2.7 31.1 1.0 OD1 G:ASN148 2.7 34.4 1.0 OD1 A:ASN148 2.8 25.4 1.0 OD1 D:ASN148 2.8 27.1 1.0 OE1 A:GLN151 2.8 28.1 1.0 OE1 G:GLN151 2.8 34.1 1.0 OE1 K:GLN151 2.9 32.6 1.0 OE1 D:GLN151 3.0 23.6 1.0 O D:HOH325 3.2 33.4 1.0 CG K:ASN148 3.6 27.3 1.0 CG G:ASN148 3.7 31.3 1.0 CG A:ASN148 3.8 26.7 1.0 CD A:GLN151 3.8 25.3 1.0 CG D:ASN148 3.8 28.6 1.0 CD G:GLN151 3.9 31.7 1.0 CD K:GLN151 3.9 27.4 1.0 CD D:GLN151 3.9 34.8 1.0 ND2 K:ASN148 4.0 34.5 1.0 NE2 D:GLN151 4.0 28.6 1.0 NE2 A:GLN151 4.1 24.1 1.0 NE2 K:GLN151 4.1 23.9 1.0 ND2 G:ASN148 4.1 34.5 1.0 NE2 G:GLN151 4.1 29.3 1.0 ND2 A:ASN148 4.2 29.9 1.0 ND2 D:ASN148 4.3 32.8 1.0 CB K:ASN148 4.8 28.1 1.0 CB A:ASN148 4.9 22.3 1.0 CB G:ASN148 4.9 26.6 1.0

Arsenic binding site 2 out of 3 in the 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ B:As201 b:23.5 occ:1.00 OD1 L:ASN148 2.6 35.5 1.0 OD1 H:ASN148 2.7 29.1 1.0 OE1 H:GLN151 2.8 31.7 1.0 OE1 B:GLN151 2.8 32.0 1.0 OE1 L:GLN151 2.9 31.6 1.0 OD1 B:ASN148 3.0 31.9 1.0 CG L:ASN148 3.6 43.0 1.0 CG H:ASN148 3.7 37.0 1.0 CG B:ASN148 3.7 36.4 1.0 CD H:GLN151 3.7 33.3 1.0 CD B:GLN151 3.8 38.0 1.0 CD L:GLN151 3.9 35.8 1.0 NE2 H:GLN151 4.0 30.6 1.0 NE2 B:GLN151 4.0 31.0 1.0 ND2 L:ASN148 4.0 37.3 1.0 ND2 B:ASN148 4.1 32.3 1.0 ND2 H:ASN148 4.1 38.4 1.0 NE2 L:GLN151 4.2 32.6 1.0 CB L:ASN148 4.8 36.2 1.0 CB B:ASN148 4.9 36.6 1.0 CB H:ASN148 4.9 35.8 1.0

Arsenic binding site 3 out of 3 in the 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of 2.20A Resolution Structure of Bfrb (L68A) From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ C:As201 b:36.8 occ:1.00 OE1 C:GLN151 2.7 42.4 1.0 OE1 E:GLN151 3.0 35.2 1.0 OD1 E:ASN148 3.0 42.8 1.0 OD1 C:ASN148 3.1 46.5 1.0 ND2 C:ASN148 3.5 44.2 1.0 CG C:ASN148 3.5 48.1 1.0 CD C:GLN151 3.7 45.2 1.0 CG E:ASN148 3.7 45.1 1.0 NE2 C:GLN151 3.9 42.9 1.0 CD E:GLN151 3.9 41.7 1.0 ND2 E:ASN148 4.1 45.9 1.0 NE2 E:GLN151 4.2 31.4 1.0 CB C:ASN148 4.7 33.0 1.0 CB E:ASN148 4.9 40.9 1.0

Y.Wang, H.Yao, Y.Cheng, S.Lovell, K.P.Battaile, C.R.Midaugh, M.Rivera. Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin Protein-Protein Interaction in Solution and Determination of Binding Energy Hot Spots. Biochemistry V. 54 6162 2015.
ISSN: ISSN 0006-2960
PubMed: 26368531
DOI: 10.1021/ACS.BIOCHEM.5B00937