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Vanadium in PDB 4usz: Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase

Enzymatic activity of Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase

All present enzymatic activity of Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase:
1.11.1.8;

Protein crystallography data

The structure of Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase, PDB code: 4usz was solved by E.Rebuffet, L.Delage, J.B.Fournier, J.Rzonca, P.Potin, G.Michel, M.Czjzek, C.Leblanc, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.04 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.840, 85.870, 116.090, 90.00, 90.00, 90.00
R / Rfree (%) 15.829 / 20.717

Other elements in 4usz:

The structure of Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase also contains other interesting chemical elements:

Sodium (Na) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase (pdb code 4usz). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total only one binding site of Vanadium was determined in the Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase, PDB code: 4usz:

Vanadium binding site 1 out of 1 in 4usz

Go back to Vanadium Binding Sites List in 4usz
Vanadium binding site 1 out of 1 in the Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of the First Bacterial Vanadium Dependant Iodoperoxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1447

b:25.3
occ:1.00
 V A:VO41447 0.0 25.3 1.0
O4 A:VO41447 1.8 16.6 1.0
O1 A:VO41447 1.8 20.0 1.0
O3 A:VO41447 1.9 18.6 1.0
O2 A:VO41447 1.9 23.8 1.0
NE2 A:HIS416 3.0 14.2 1.0
NH2 A:ARG410 3.4 16.0 1.0
N A:GLY359 3.5 8.6 1.0
ND1 A:HIS360 3.7 13.6 1.0
NH2 A:ARG331 3.8 8.6 1.0
CE1 A:HIS416 3.8 11.5 1.0
CE1 A:PHE353 3.9 9.1 1.0
CD2 A:HIS416 4.0 14.1 1.0
OG A:SER358 4.0 8.3 1.0
NE A:ARG410 4.1 12.6 1.0
NZ A:LYS324 4.1 5.4 1.0
N A:HIS360 4.1 10.0 1.0
CZ A:ARG410 4.2 13.8 1.0
NH1 A:ARG331 4.2 9.1 1.0
CA A:SER358 4.2 9.1 1.0
C A:SER358 4.3 8.8 1.0
CA A:GLY359 4.3 9.2 1.0
CE1 A:HIS360 4.4 15.0 1.0
O A:HOH2283 4.4 16.3 1.0
CZ A:ARG331 4.5 9.3 1.0
CZ A:PHE353 4.5 8.5 1.0
CE A:LYS324 4.6 6.0 1.0
CG A:HIS360 4.7 12.5 1.0
CB A:SER358 4.7 8.6 1.0
C A:GLY359 4.7 10.0 1.0
CG A:PRO351 4.8 12.7 1.0
CB A:HIS360 4.9 10.8 1.0
CD1 A:PHE353 4.9 9.0 1.0

Reference:

J.B.Fournier, E.Rebuffet, L.Delage, R.Grijol, L.Meslet-Cladiere, J.Rzonca, P.Potin, G.Michel, M.Czjzek, C.Leblanc. The Bacterial Vanadium Iodoperoxidase From the Marine Flavobacteriaceae Zobellia Galactanivorans Reveals Novel Molecular and Evolutionary Features of Halide Specificity in This Enzyme Family. Appl.Environ.Microbiol. 2014.
ISSN: ESSN 1098-5336
PubMed: 25261522
DOI: 10.1128/AEM.02430-14
Page generated: Wed Dec 16 02:31:18 2020

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