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Vanadium in PDB 2azd: X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family

Enzymatic activity of X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family

All present enzymatic activity of X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family:
2.4.1.1;

Protein crystallography data

The structure of X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family, PDB code: 2azd was solved by S.Geremia, M.Campagnolo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.83 / 2.16
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.779, 105.892, 220.230, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 25

Vanadium Binding Sites:

The binding sites of Vanadium atom in the X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family (pdb code 2azd). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family, PDB code: 2azd:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 2azd

Go back to Vanadium Binding Sites List in 2azd
Vanadium binding site 1 out of 2 in the X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V999

b:82.8
occ:1.00
V A:VO4999 0.0 82.8 1.0
O1 A:VO4999 1.5 76.0 1.0
O3 A:VO4999 1.5 77.4 1.0
O4 A:VO4999 1.5 76.2 1.0
O2 A:VO4999 1.5 75.1 1.0
NH2 A:ARG534 3.6 55.9 1.0
C6 A:GLC997 3.7 75.9 1.0
O1P A:PLP900 3.8 34.7 1.0
N A:GLY114 3.9 28.9 1.0
NZ A:LYS539 3.9 42.0 1.0
O4 A:GLC997 3.9 76.0 1.0
O A:HOH1326 4.1 53.1 1.0
NE A:ARG534 4.1 51.4 1.0
CZ A:ARG534 4.3 55.0 1.0
CA A:GLY114 4.3 28.6 1.0
C5 A:GLC997 4.4 76.8 1.0
C3 A:TRS990 4.5 50.4 1.0
O3 A:TRS990 4.7 55.2 1.0
O6 A:GLC997 4.7 73.3 1.0
CE A:LYS539 4.7 41.3 1.0
O A:HOH1267 4.7 37.4 1.0
C4 A:GLC997 4.8 77.5 1.0
P A:PLP900 4.9 35.1 1.0
C A:GLY113 4.9 29.6 1.0

Vanadium binding site 2 out of 2 in 2azd

Go back to Vanadium Binding Sites List in 2azd
Vanadium binding site 2 out of 2 in the X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of X-Ray Studies on Maltodextrin Phosphorylase (Malp) Complexes: Recognition of Substrates and Catalytic Mechanism of Phosphorylase Family within 5.0Å range:
probe atom residue distance (Å) B Occ
B:V1999

b:83.2
occ:1.00
V B:VO41999 0.0 83.2 1.0
O1 B:VO41999 1.5 76.2 1.0
O3 B:VO41999 1.5 77.8 1.0
O2 B:VO41999 1.5 75.3 1.0
O4 B:VO41999 1.5 76.6 1.0
NH2 B:ARG534 3.5 56.7 1.0
O B:HOH2223 3.6 51.2 1.0
O4 B:GLC997 3.7 75.6 1.0
C6 B:GLC997 3.7 76.2 1.0
N B:GLY114 3.9 28.9 1.0
NZ B:LYS539 4.0 42.1 1.0
O1P B:PLP900 4.0 40.1 1.0
NE B:ARG534 4.2 52.3 1.0
O B:HOH2091 4.3 71.8 1.0
C3 B:TRS1990 4.3 50.4 1.0
CZ B:ARG534 4.3 54.6 1.0
CA B:GLY114 4.3 28.8 1.0
C5 B:GLC997 4.4 76.9 1.0
C4 B:GLC997 4.6 77.7 1.0
O2P B:PLP900 4.7 38.8 1.0
O3 B:TRS1990 4.8 53.6 1.0
CE B:LYS539 4.8 41.5 1.0
O6 B:GLC997 4.8 73.5 1.0
P B:PLP900 4.9 37.4 1.0

Reference:

M.Campagnolo, C.Campa, R.D.Zorzi, J.Wuerges, S.Geremia. X-Ray Studies on Ternary Complexes of Maltodextrin Phosphorylase. Arch.Biochem.Biophys. V. 471 11 2008.
ISSN: ISSN 0003-9861
PubMed: 18164678
DOI: 10.1016/J.ABB.2007.11.023
Page generated: Wed Dec 16 02:30:39 2020

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