Vanadium in PDB 3zwu: Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue

All present enzymatic activity of Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue:
3.1.3.1;

The structure of Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue, PDB code: 3zwu was solved by S.C.Yong, P.Roversi, J.E.D.Lillington, O.B.Zeldin, E.F.Garman, S.M.Lea, B.C.Berks, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.42 / 1.39
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.790, 71.470, 227.830, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 17.13

The structure of Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Chlorine	(Cl)	4 atoms
Calcium	(Ca)	6 atoms

The binding sites of Vanadium atom in the Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue (pdb code 3zwu). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue, PDB code: 3zwu:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in the Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:V700 b:14.6 occ:0.66 V A:VO4700 0.0 14.6 0.7 O3 A:VO4700 1.7 9.0 0.7 O4 A:VO4700 1.7 12.3 0.7 O1 A:VO4700 1.7 12.0 0.7 O2 A:VO4700 1.8 8.2 0.7 O A:FEO1594 2.3 8.8 1.0 FE1 A:FEO1594 3.0 9.8 1.0 CA A:CA1593 3.1 10.6 0.7 FE2 A:FEO1594 3.2 10.0 1.0 CA A:CA1592 3.4 10.0 0.9 O A:HOH2196 3.4 11.1 1.0 O A:HOH2721 3.5 17.3 1.0 O A:HOH2244 3.6 11.3 1.0 OE2 A:GLU387 3.6 11.1 1.0 CA A:CA1591 3.7 9.7 0.9 O A:HOH2481 3.7 24.7 1.0 O A:HOH2245 3.8 24.9 1.0 OE1 A:GLU194 3.9 10.1 1.0 OD2 A:ASP494 4.0 13.5 1.0 OE2 A:GLU194 4.0 9.7 1.0 O A:HOH2910 4.1 31.1 1.0 OD2 A:ASP292 4.2 10.7 1.0 CD A:GLU194 4.4 14.6 1.0 NH2 A:ARG385 4.4 19.2 1.0 OD2 A:ASP479 4.4 10.3 1.0 OE2 A:GLU90 4.4 9.2 1.0 O A:HOH2252 4.7 16.7 1.0 OE1 A:GLU90 4.7 10.8 1.0 OE2 A:GLU532 4.7 12.8 1.0 CD A:GLU387 4.7 16.0 1.0 OD1 A:ASN195 4.8 18.5 1.0 O A:HOH2832 4.9 28.5 1.0 OE1 A:GLU273 5.0 10.1 1.0

Vanadium binding site 2 out of 2 in the Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Pseudomonas Fluorescens Phox in Complex with Vanadate, A Transition State Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:V700 b:13.3 occ:0.66 V B:VO4700 0.0 13.3 0.7 O4 B:VO4700 1.7 10.8 0.7 O3 B:VO4700 1.7 8.2 0.7 O2 B:VO4700 1.8 9.8 0.7 O1 B:VO4700 1.8 11.0 0.7 O B:FEO1594 2.4 9.9 1.0 FE1 B:FEO1594 3.1 9.3 1.0 CA B:CA1593 3.1 11.2 0.7 FE2 B:FEO1594 3.2 9.4 1.0 CA B:CA1592 3.4 10.6 1.0 O B:HOH2620 3.4 14.5 1.0 O B:HOH2180 3.4 10.6 1.0 OE2 B:GLU387 3.6 9.7 1.0 O B:HOH2213 3.6 10.4 1.0 CA B:CA1591 3.7 10.1 1.0 O B:HOH2212 3.8 21.9 1.0 O B:HOH2407 3.9 28.2 1.0 OE1 B:GLU194 3.9 9.2 1.0 OD2 B:ASP494 4.0 12.6 1.0 OE2 B:GLU194 4.0 10.2 1.0 O B:HOH2798 4.1 28.4 1.0 OD2 B:ASP292 4.2 10.5 1.0 CD B:GLU194 4.4 11.8 1.0 NH2 B:ARG385 4.4 17.2 1.0 OD2 B:ASP479 4.4 10.4 1.0 OE2 B:GLU90 4.4 8.7 1.0 O B:HOH2217 4.6 17.1 1.0 OE1 B:GLU90 4.7 10.1 1.0 OE2 B:GLU532 4.7 10.8 1.0 CD B:GLU387 4.7 12.8 1.0 OD1 B:ASN195 4.8 18.8 1.0 O B:HOH2724 4.9 19.1 1.0 OE1 B:GLU273 4.9 9.1 1.0 OE2 B:GLU273 5.0 10.0 1.0

S.C.Yong, P.Roversi, J.Lillington, F.Rodriguez, M.Krehenbrink, O.B.Zeldin, E.F.Garman, S.M.Lea, B.C.Berks. A Complex Iron-Calcium Cofactor Catalyzing Phosphotransfer Chemistry Science V. 345 1170 2014.
ISSN: ISSN 0036-8075
PubMed: 25190793
DOI: 10.1126/SCIENCE.1254237