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Vanadium in PDB 4ae3: Crystal Structure of Ammosamide 272:Myosin-2 Motor Domain Complex

Enzymatic activity of Crystal Structure of Ammosamide 272:Myosin-2 Motor Domain Complex

All present enzymatic activity of Crystal Structure of Ammosamide 272:Myosin-2 Motor Domain Complex:
3.6.4.1;

Protein crystallography data

The structure of Crystal Structure of Ammosamide 272:Myosin-2 Motor Domain Complex, PDB code: 4ae3 was solved by K.Chinthalapudi, S.M.Heissler, W.Fenical, D.J.Manstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.914 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 88.050, 145.520, 153.830, 90.00, 90.00, 90.00
R / Rfree (%) 21.38 / 25.36

Other elements in 4ae3:

The structure of Crystal Structure of Ammosamide 272:Myosin-2 Motor Domain Complex also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of Ammosamide 272:Myosin-2 Motor Domain Complex (pdb code 4ae3). 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 Ammosamide 272:Myosin-2 Motor Domain Complex, PDB code: 4ae3:

Vanadium binding site 1 out of 1 in 4ae3

Go back to Vanadium Binding Sites List in 4ae3
Vanadium binding site 1 out of 1 in the Crystal Structure of Ammosamide 272:Myosin-2 Motor Domain 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 Ammosamide 272:Myosin-2 Motor Domain Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1750

b:22.9
occ:1.00
 VG A:AOV1750 0.0 22.9 1.0
O1G A:AOV1750 1.7 19.8 1.0
O3G A:AOV1750 1.8 20.4 1.0
O2G A:AOV1750 1.8 18.2 1.0
O4G A:AOV1750 1.8 28.4 1.0
O3B A:AOV1750 2.1 22.1 1.0
MG A:MG1751 3.2 23.8 1.0
PB A:AOV1750 3.4 26.0 1.0
OG A:SER181 3.8 22.9 1.0
CA A:SER181 3.8 22.0 1.0
N A:GLY182 3.9 20.8 1.0
O1B A:AOV1750 3.9 23.8 1.0
OG A:SER236 3.9 17.2 1.0
O A:HOH2197 3.9 23.1 1.0
N A:GLY457 3.9 17.4 1.0
ND2 A:ASN233 4.0 18.5 1.0
NZ A:LYS185 4.0 16.3 1.0
N A:SER237 4.1 20.6 1.0
O2B A:AOV1750 4.1 22.2 1.0
CB A:SER181 4.2 24.6 1.0
C A:SER181 4.4 21.7 1.0
CA A:SER236 4.4 24.2 1.0
CE A:LYS185 4.6 17.7 1.0
O A:SER237 4.6 25.2 1.0
CB A:SER236 4.7 23.6 1.0
O3A A:AOV1750 4.7 28.3 1.0
O A:HOH2163 4.7 20.2 1.0
CA A:SER456 4.7 21.5 1.0
CA A:GLY457 4.7 20.5 1.0
CB A:SER237 4.7 18.0 1.0
O A:HOH2164 4.7 19.4 1.0
C A:SER236 4.7 19.9 1.0
C A:SER456 4.8 18.9 1.0
N A:SER181 4.9 19.9 1.0
CA A:SER237 4.9 22.1 1.0
OG A:SER237 5.0 26.0 1.0
CA A:GLY182 5.0 21.2 1.0

Reference:

K.Chinthalapudi, S.M.Heissler, W.Fenical, D.J.Manstein. Structural Basis For Ammosamide Mediated Myosin Motor Activity Inhibition To Be Published.
Page generated: Fri Oct 11 19:31:05 2024

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