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Vanadium in PDB 7b19: Mutant Myosin-II-Ggg Motor Domain

Protein crystallography data

The structure of Mutant Myosin-II-Ggg Motor Domain, PDB code: 7b19 was solved by W.Ewert, M.Preller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.59 / 2.55
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.187, 149.031, 153.93, 90, 90, 90
R / Rfree (%) 20.6 / 25.2

Other elements in 7b19:

The structure of Mutant Myosin-II-Ggg Motor Domain also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Mutant Myosin-II-Ggg Motor Domain (pdb code 7b19). 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 Mutant Myosin-II-Ggg Motor Domain, PDB code: 7b19:

Vanadium binding site 1 out of 1 in 7b19

Go back to Vanadium Binding Sites List in 7b19
Vanadium binding site 1 out of 1 in the Mutant Myosin-II-Ggg Motor Domain


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Mutant Myosin-II-Ggg Motor Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V801

b:25.4
occ:1.00
VG A:AD9801 0.0 25.4 1.0
O2G A:AD9801 1.9 33.7 1.0
O1G A:AD9801 1.9 34.2 1.0
O3G A:AD9801 2.0 45.1 1.0
O3B A:AD9801 2.0 47.0 1.0
H2G1 A:AD9801 2.2 40.5 1.0
H3G1 A:AD9801 2.3 54.1 1.0
O A:HOH906 2.6 48.9 1.0
HA A:SER181 2.8 47.4 1.0
HD22 A:ASN233 3.0 46.3 1.0
HZ1 A:LYS185 3.0 41.9 1.0
H A:GLY182 3.0 36.7 1.0
PB A:AD9801 3.1 32.3 1.0
O1B A:AD9801 3.3 40.7 1.0
H A:SER237 3.4 41.5 1.0
HG A:SER236 3.4 50.4 1.0
H A:GLY457 3.4 38.6 1.0
HA A:SER236 3.5 48.3 1.0
MG A:MG802 3.6 39.7 1.0
HG A:SER181 3.6 37.0 1.0
CA A:SER181 3.7 39.5 1.0
ND2 A:ASN233 3.7 38.5 1.0
OG A:SER181 3.7 30.8 1.0
N A:GLY182 3.8 30.5 1.0
NZ A:LYS185 3.8 34.9 1.0
O2B A:AD9801 4.0 36.2 1.0
HD21 A:ASN233 4.0 46.3 1.0
HZ3 A:LYS185 4.0 41.9 1.0
O3A A:AD9801 4.1 44.1 1.0
OG A:SER236 4.1 42.0 1.0
CB A:SER181 4.1 28.2 1.0
HA A:SER456 4.1 46.5 1.0
N A:SER237 4.2 34.6 1.0
O A:HOH917 4.2 26.4 1.0
HB2 A:SER181 4.2 33.9 1.0
N A:GLY457 4.3 32.2 1.0
C A:SER181 4.3 30.3 1.0
O A:HOH902 4.3 38.3 1.0
HZ2 A:LYS185 4.3 41.9 1.0
HB2 A:SER237 4.3 48.8 1.0
CA A:SER236 4.4 40.2 1.0
HE2 A:LYS185 4.4 43.9 1.0
HA3 A:GLY457 4.6 47.3 1.0
HB3 A:ASN233 4.6 44.9 1.0
CE A:LYS185 4.6 36.6 1.0
HA2 A:GLY182 4.7 54.9 1.0
CB A:SER236 4.7 34.8 1.0
HB2 A:ASN233 4.7 44.9 1.0
HB2 A:SER236 4.8 41.8 1.0
N A:SER181 4.8 32.2 1.0
O A:SER237 4.8 38.1 1.0
HE3 A:LYS185 4.8 43.9 1.0
C A:SER236 4.8 39.1 1.0
CG A:ASN233 4.8 41.0 1.0
CA A:GLY182 4.9 45.8 1.0
OG A:SER237 4.9 35.7 1.0
CB A:SER237 4.9 40.6 1.0
O A:GLU180 5.0 26.7 1.0
CB A:ASN233 5.0 37.4 1.0

Reference:

P.Franz, W.Ewert, M.Preller, G.Tsiavaliaris. Unraveling A Force-Generating Allosteric Pathway of Actomyosin Communication Associated with Adp and P I Release. Int J Mol Sci V. 22 2020.
ISSN: ESSN 1422-0067
PubMed: 33374308
DOI: 10.3390/IJMS22010104
Page generated: Mon Jan 25 16:05:47 2021

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