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Vanadium in PDB 4zg4: Myosin Vc Pre-Powerstroke

Protein crystallography data

The structure of Myosin Vc Pre-Powerstroke, PDB code: 4zg4 was solved by V.Ropars, O.Pylypenko, L.Sweeney, A.Houdusse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.54 / 2.36
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 118.280, 67.320, 133.180, 90.00, 108.48, 90.00
R / Rfree (%) 17.3 / 21.3

Other elements in 4zg4:

The structure of Myosin Vc Pre-Powerstroke also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Myosin Vc Pre-Powerstroke (pdb code 4zg4). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Myosin Vc Pre-Powerstroke, PDB code: 4zg4:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 4zg4

Go back to Vanadium Binding Sites List in 4zg4
Vanadium binding site 1 out of 2 in the Myosin Vc Pre-Powerstroke


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Myosin Vc Pre-Powerstroke within 5.0Å range:
probe atom residue distance (Å) B Occ
B:V802

b:42.1
occ:1.00
V B:VO4802 0.0 42.1 1.0
O3 B:VO4802 1.7 54.6 1.0
O2 B:VO4802 1.7 47.5 1.0
O1 B:VO4802 1.7 41.2 1.0
O4 B:VO4802 1.9 42.1 1.0
O3B B:ADP803 2.0 50.2 1.0
HG B:SER163 3.1 61.9 1.0
H B:SER216 3.1 49.1 1.0
HD22 B:ASN212 3.1 49.4 1.0
HA B:SER163 3.2 51.2 1.0
HG B:SER215 3.2 52.0 1.0
H B:GLY164 3.2 42.2 1.0
PB B:ADP803 3.3 47.9 1.0
HZ1 B:LYS167 3.3 44.8 1.0
H B:GLY438 3.3 55.7 1.0
HA B:SER215 3.5 66.0 1.0
MG B:MG801 3.5 44.7 1.0
O1B B:ADP803 3.5 35.9 1.0
HA B:TYR437 3.7 56.1 1.0
N B:SER216 3.9 40.9 1.0
O B:HOH1011 3.9 42.1 1.0
OG B:SER163 3.9 51.6 1.0
O B:HOH920 3.9 44.1 1.0
ND2 B:ASN212 4.0 41.1 1.0
OG B:SER215 4.0 43.3 1.0
N B:GLY164 4.0 35.1 1.0
CA B:SER163 4.0 42.6 1.0
HB2 B:SER216 4.1 51.3 1.0
NZ B:LYS167 4.1 37.3 1.0
N B:GLY438 4.2 46.4 1.0
O2B B:ADP803 4.2 41.7 1.0
HD21 B:ASN212 4.2 49.4 1.0
HZ3 B:LYS167 4.2 44.8 1.0
O B:HOH918 4.3 38.3 1.0
CA B:SER215 4.3 55.0 1.0
O3A B:ADP803 4.3 51.5 1.0
HE2 B:LYS167 4.3 49.1 1.0
CB B:SER163 4.4 51.8 1.0
HB2 B:SER163 4.4 62.2 1.0
O B:SER216 4.5 46.4 1.0
C B:SER163 4.6 42.9 1.0
OG B:SER216 4.6 38.8 1.0
CB B:SER215 4.6 52.8 1.0
CA B:TYR437 4.6 46.8 1.0
C B:SER215 4.6 54.1 1.0
CB B:SER216 4.6 42.8 1.0
HB2 B:SER215 4.7 63.4 1.0
HB3 B:ASN212 4.7 43.6 1.0
HB3 B:TYR437 4.7 52.3 1.0
CE B:LYS167 4.7 40.9 1.0
HZ2 B:LYS167 4.7 44.8 1.0
CA B:SER216 4.7 42.8 1.0
HA3 B:GLY438 4.8 43.1 1.0
HA2 B:GLY164 4.8 50.9 1.0
HE3 B:LYS167 4.9 49.1 1.0
HB2 B:ASN212 4.9 43.6 1.0
C B:TYR437 4.9 49.0 1.0
HH11 B:ARG217 5.0 52.5 1.0

Vanadium binding site 2 out of 2 in 4zg4

Go back to Vanadium Binding Sites List in 4zg4
Vanadium binding site 2 out of 2 in the Myosin Vc Pre-Powerstroke


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Myosin Vc Pre-Powerstroke within 5.0Å range:
probe atom residue distance (Å) B Occ
E:V802

b:51.9
occ:1.00
V E:VO4802 0.0 51.9 1.0
O1 E:VO4802 1.7 50.7 1.0
O3 E:VO4802 1.7 45.7 1.0
O2 E:VO4802 1.7 55.2 1.0
O4 E:VO4802 1.9 51.2 1.0
O3B E:ADP803 1.9 57.6 1.0
HG E:SER163 3.0 65.2 1.0
HG E:SER215 3.1 69.7 1.0
H E:SER216 3.1 56.3 1.0
HA E:SER163 3.2 56.3 1.0
HD22 E:ASN212 3.2 52.2 1.0
H E:GLY164 3.2 53.8 1.0
HZ1 E:LYS167 3.2 53.7 1.0
PB E:ADP803 3.2 54.1 1.0
H E:GLY438 3.2 59.0 1.0
HA E:SER215 3.5 60.5 1.0
MG E:MG801 3.5 53.6 1.0
O1B E:ADP803 3.5 46.2 1.0
HA E:TYR437 3.6 58.7 1.0
OG E:SER163 3.8 54.3 1.0
N E:SER216 3.8 46.9 1.0
OG E:SER215 3.8 58.1 1.0
O E:HOH1007 3.9 58.6 1.0
HB2 E:SER216 3.9 52.7 1.0
O E:HOH969 3.9 51.9 1.0
N E:GLY164 4.0 44.8 1.0
ND2 E:ASN212 4.0 43.5 1.0
CA E:SER163 4.0 46.9 1.0
NZ E:LYS167 4.0 44.8 1.0
O2B E:ADP803 4.1 48.9 1.0
N E:GLY438 4.1 49.2 1.0
HZ3 E:LYS167 4.1 53.7 1.0
O E:HOH952 4.3 49.1 1.0
CA E:SER215 4.3 50.4 1.0
HD21 E:ASN212 4.3 52.2 1.0
HB2 E:SER163 4.3 58.4 1.0
CB E:SER163 4.3 48.6 1.0
O3A E:ADP803 4.3 48.3 1.0
HE2 E:LYS167 4.4 53.4 1.0
O E:SER216 4.4 53.2 1.0
CA E:TYR437 4.5 49.0 1.0
CB E:SER216 4.5 43.9 1.0
CB E:SER215 4.6 52.6 1.0
OG E:SER216 4.6 47.1 1.0
C E:SER215 4.6 59.0 1.0
C E:SER163 4.6 49.7 1.0
HB3 E:TYR437 4.6 58.0 1.0
HZ2 E:LYS167 4.6 53.7 1.0
CA E:SER216 4.7 50.4 1.0
HA3 E:GLY438 4.7 56.6 1.0
HB3 E:ASN212 4.7 52.4 1.0
CE E:LYS167 4.7 44.5 1.0
HB2 E:SER215 4.7 63.1 1.0
HA2 E:GLY164 4.8 59.9 1.0
C E:TYR437 4.9 57.8 1.0
HE3 E:LYS167 4.9 53.4 1.0
HB2 E:ASN212 4.9 52.4 1.0
CA E:GLY438 5.0 47.1 1.0

Reference:

S.F.Wulf, V.Ropars, S.Fujita-Becker, M.Oster, G.Hofhaus, L.G.Trabuco, O.Pylypenko, H.L.Sweeney, A.M.Houdusse, R.R.Schroder. Force-Producing Adp State of Myosin Bound to Actin. Proc.Natl.Acad.Sci.Usa V. 113 E1844 2016.
ISSN: ESSN 1091-6490
PubMed: 26976594
DOI: 10.1073/PNAS.1516598113
Page generated: Thu Oct 29 07:05:38 2020

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