Iron in PDB 7r3f: Monomeric Pqse Mutant E187R

All present enzymatic activity of Monomeric Pqse Mutant E187R:
3.1.2.32;

The structure of Monomeric Pqse Mutant E187R, PDB code: 7r3f was solved by S.R.Borgert, S.Schmelz, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.29 / 1.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.535, 60.174, 128.262, 90, 90, 90
R / Rfree (%)	20.4 / 23.9

The structure of Monomeric Pqse Mutant E187R also contains other interesting chemical elements:

Arsenic

(As)

1 atom

The binding sites of Iron atom in the Monomeric Pqse Mutant E187R (pdb code 7r3f). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Monomeric Pqse Mutant E187R, PDB code: 7r3f:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Monomeric Pqse Mutant E187R


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Monomeric Pqse Mutant E187R within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:10.3 occ:1.00 O A:HOH514 1.9 10.0 1.0 NE2 A:HIS176 2.1 6.3 1.0 ND1 A:HIS88 2.3 7.7 1.0 NE2 A:HIS86 2.3 7.8 1.0 O2 A:CAC403 2.3 27.0 1.0 OD2 A:ASP195 2.4 8.5 1.0 CE1 A:HIS176 3.0 6.5 1.0 HE1 A:HIS176 3.1 7.8 1.0 CE1 A:HIS88 3.1 8.5 1.0 CD2 A:HIS176 3.2 9.2 1.0 HB2 A:HIS88 3.2 7.2 1.0 CD2 A:HIS86 3.2 9.5 1.0 HE1 A:HIS88 3.3 10.2 1.0 CE1 A:HIS86 3.3 6.7 1.0 CG A:HIS88 3.3 9.7 1.0 HD2 A:HIS86 3.4 11.4 1.0 HB2 A:ASP195 3.4 5.6 1.0 HE1 A:HIS86 3.4 8.0 1.0 HD2 A:HIS176 3.4 11.0 1.0 CG A:ASP195 3.4 8.8 1.0 FE A:FE402 3.5 11.4 1.0 AS A:CAC403 3.6 29.4 1.0 CB A:HIS88 3.7 6.0 1.0 HB3 A:HIS88 3.8 7.2 1.0 HD2 A:HIS91 3.8 10.4 1.0 CB A:ASP195 3.8 4.7 1.0 O1 A:CAC403 3.9 14.5 1.0 HB3 A:ASP195 4.0 5.6 1.0 NE2 A:HIS91 4.1 7.6 1.0 CD2 A:HIS91 4.1 8.7 1.0 ND1 A:HIS176 4.2 7.2 1.0 NE2 A:HIS88 4.3 10.2 1.0 CG A:HIS176 4.3 7.5 1.0 ND1 A:HIS86 4.4 8.5 1.0 O A:HOH668 4.4 23.3 1.0 CD2 A:HIS88 4.4 10.2 1.0 CG A:HIS86 4.4 7.9 1.0 OD1 A:ASP90 4.5 9.3 1.0 C2 A:CAC403 4.5 14.6 1.0 OD1 A:ASP195 4.5 7.6 1.0 HD2 A:HIS180 4.8 10.1 1.0 HD2 A:PHE212 4.8 15.8 1.0 HD13 A:LEU210 4.8 14.5 1.0 OD2 A:ASP90 4.9 9.0 1.0 HD1 A:HIS176 4.9 8.6 1.0 H A:HIS88 5.0 9.6 1.0

Iron binding site 2 out of 2 in the Monomeric Pqse Mutant E187R


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Monomeric Pqse Mutant E187R within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:11.4 occ:1.00 O1 A:CAC403 2.0 14.5 1.0 NE2 A:HIS238 2.1 7.6 1.0 NE2 A:HIS91 2.2 7.6 1.0 O A:HOH514 2.3 10.0 1.0 OD2 A:ASP90 2.3 9.0 1.0 OD2 A:ASP195 2.3 8.5 1.0 CD2 A:HIS91 3.1 8.7 1.0 CE1 A:HIS238 3.1 8.4 1.0 CG A:ASP195 3.1 8.8 1.0 HD2 A:HIS91 3.2 10.4 1.0 CD2 A:HIS238 3.2 9.6 1.0 HE1 A:HIS238 3.2 10.1 1.0 AS A:CAC403 3.2 29.4 1.0 CE1 A:HIS91 3.2 7.0 1.0 CG A:ASP90 3.3 7.4 1.0 OD1 A:ASP195 3.3 7.6 1.0 HD2 A:HIS238 3.4 11.5 1.0 FE A:FE401 3.5 10.3 1.0 HE1 A:HIS91 3.5 8.4 1.0 OD1 A:ASP90 3.6 9.3 1.0 O2 A:CAC403 3.7 27.0 1.0 C2 A:CAC403 3.8 14.6 1.0 HE1 A:HIS86 3.9 8.0 1.0 ND1 A:HIS238 4.2 9.3 1.0 CG A:HIS91 4.3 7.5 1.0 HE1 A:PHE293 4.3 12.9 1.0 CG A:HIS238 4.3 6.2 1.0 ND1 A:HIS91 4.3 5.8 1.0 NE2 A:HIS86 4.5 7.8 1.0 CE1 A:HIS86 4.5 6.7 1.0 HB2 A:ASP90 4.5 11.5 1.0 CB A:ASP90 4.6 9.6 1.0 CB A:ASP195 4.6 4.7 1.0 HB2 A:ASP195 4.8 5.6 1.0 HB2 A:HIS88 4.8 7.2 1.0 HB3 A:ASP195 4.8 5.6 1.0 C1 A:CAC403 4.9 16.0 1.0 HA3 A:GLY237 4.9 11.2 1.0 HD1 A:HIS238 5.0 11.2 1.0

S.R.Borgert, S.Henke, F.Witzgall, S.Schmelz, S.Zur Lage, S.K.Hotop, S.Stephen, D.Lubken, J.Kruger, N.O.Gomez, M.Van Ham, L.Jansch, M.Kalesse, A.Pich, M.Bronstrup, S.Haussler, W.Blankenfeldt. Moonlighting Chaperone Activity of the Enzyme Pqse Contributes to Rhlr-Controlled Virulence of Pseudomonas Aeruginosa. Nat Commun V. 13 7402 2022.
ISSN: ESSN 2041-1723
PubMed: 36456567
DOI: 10.1038/S41467-022-35030-W