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Vanadium in PDB 5bzx: Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex

Enzymatic activity of Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex

All present enzymatic activity of Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex:
3.1.3.16; 3.1.3.48; 3.1.3.67;

Protein crystallography data

The structure of Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex, PDB code: 5bzx was solved by C.-U.Lee, D.Bier, S.Hennig, T.N.Grossmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.29 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 207.060, 206.900, 87.670, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 20.4

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex (pdb code 5bzx). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex, PDB code: 5bzx:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 5bzx

Go back to Vanadium Binding Sites List in 5bzx
Vanadium binding site 1 out of 2 in the Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex


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 Human Phosphatase Pten Treated with A Bisperoxovanadium Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V401

b:90.1
occ:0.80
V A:VO4401 0.0 90.1 0.8
O2 A:VO4401 1.9 88.3 0.8
O1 A:VO4401 1.9 87.0 0.8
O3 A:VO4401 1.9 77.1 0.8
O4 A:VO4401 1.9 70.0 0.8
N A:LYS128 3.3 67.9 1.0
N A:GLY127 3.5 74.8 1.0
O A:HOH507 3.8 63.5 1.0
CA A:GLY127 4.0 73.5 1.0
N A:ARG130 4.0 42.8 1.0
N A:GLY129 4.0 49.5 1.0
N A:ALA126 4.1 75.6 1.0
C A:GLY127 4.1 74.4 1.0
O A:HOH563 4.2 51.3 1.0
CA A:LYS128 4.2 62.7 1.0
N A:LYS125 4.2 69.4 1.0
CB A:ARG130 4.2 47.4 1.0
NE A:ARG130 4.2 52.4 1.0
OG1 A:THR131 4.3 51.1 1.0
C A:LYS128 4.3 54.9 1.0
CB A:CYS124 4.4 63.0 1.0
C A:ALA126 4.4 74.9 1.0
N A:THR131 4.5 46.5 1.0
CB A:LYS128 4.5 66.8 1.0
CA A:ALA126 4.6 76.1 1.0
CB A:ALA126 4.6 77.8 1.0
CG A:ARG130 4.7 48.5 1.0
CA A:ARG130 4.7 44.6 1.0
N A:CYS124 4.7 56.7 1.0
O A:HOH551 4.7 49.4 1.0
NH2 A:ARG130 4.8 55.1 1.0
C A:LYS125 4.8 77.4 1.0
O A:HOH612 4.8 61.3 1.0
CA A:CYS124 4.8 60.5 1.0
C A:GLY129 4.9 44.1 1.0
CA A:GLY129 4.9 44.8 1.0
C A:CYS124 4.9 66.6 1.0
CA A:LYS125 4.9 77.7 1.0
CZ A:ARG130 5.0 53.9 1.0
CD A:ARG130 5.0 50.5 1.0

Vanadium binding site 2 out of 2 in 5bzx

Go back to Vanadium Binding Sites List in 5bzx
Vanadium binding site 2 out of 2 in the Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Crystal Structure of Human Phosphatase Pten Treated with A Bisperoxovanadium Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:V402

b:68.7
occ:0.30
V C:VO4402 0.0 68.7 0.3
C1 C:TLA401 0.6 64.8 0.7
O1 C:TLA401 1.0 56.0 0.7
O11 C:TLA401 1.5 69.8 0.7
C2 C:TLA401 1.8 63.3 0.7
O2 C:VO4402 1.9 65.8 0.3
O3 C:VO4402 1.9 66.0 0.3
O4 C:VO4402 1.9 65.2 0.3
O1 C:VO4402 1.9 65.8 0.3
O2 C:TLA401 2.4 63.4 0.7
C3 C:TLA401 3.0 63.1 0.7
N C:LYS128 3.1 63.5 1.0
N C:GLY127 3.3 68.3 1.0
CA C:GLY127 3.6 65.9 1.0
OG1 C:THR131 3.7 50.5 1.0
O3 C:TLA401 3.7 64.3 0.7
C C:GLY127 3.8 63.3 1.0
N C:ARG130 4.1 45.5 1.0
CA C:LYS128 4.1 63.9 1.0
N C:GLY129 4.1 53.4 1.0
N C:THR131 4.1 48.8 1.0
N C:LYS125 4.2 59.4 1.0
N C:ALA126 4.2 60.9 1.0
C4 C:TLA401 4.2 63.9 0.7
CB C:CYS124 4.2 57.2 1.0
CB C:ARG130 4.2 49.5 1.0
C C:LYS128 4.3 57.9 1.0
N C:CYS124 4.3 50.1 1.0
C C:ALA126 4.3 70.3 1.0
NE C:ARG130 4.5 55.2 1.0
CB C:LYS128 4.5 64.7 1.0
CB C:THR131 4.6 46.8 1.0
CA C:CYS124 4.6 55.8 1.0
O4 C:TLA401 4.6 62.6 0.7
CA C:ARG130 4.6 47.5 1.0
CA C:ALA126 4.7 67.6 1.0
C C:CYS124 4.8 57.7 1.0
C C:LYS125 4.8 59.2 1.0
CB C:ALA126 4.8 72.9 1.0
CG C:ARG130 4.8 49.3 1.0
O C:GLY127 4.9 68.5 1.0
C C:ARG130 4.9 47.7 1.0
C C:GLY129 4.9 49.3 1.0
O C:LYS128 4.9 49.3 1.0
CA C:THR131 5.0 46.0 1.0
CA C:LYS125 5.0 59.6 1.0

Reference:

C.U.Lee, G.Hahne, J.Hanske, T.Bange, D.Bier, C.Rademacher, S.Hennig, T.N.Grossmann. Redox Modulation of Pten Phosphatase Activity By Hydrogen Peroxide and Bisperoxidovanadium Complexes. Angew.Chem.Int.Ed.Engl. V. 54 13796 2015.
ISSN: ESSN 1521-3773
PubMed: 26418532
DOI: 10.1002/ANIE.201506338
Page generated: Thu Oct 29 07:05:47 2020

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