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Vanadium in PDB 3myh: Insights Into the Importance of Hydrogen Bonding in the Gamma- Phosphate Binding Pocket of Myosin: Structural and Functional Studies of SER236

Protein crystallography data

The structure of Insights Into the Importance of Hydrogen Bonding in the Gamma- Phosphate Binding Pocket of Myosin: Structural and Functional Studies of SER236, PDB code: 3myh was solved by J.J.Frye, V.A.Klenchin, C.R.Bagshaw, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.62 / 2.01
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 88.430, 146.440, 153.760, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 24

Other elements in 3myh:

The structure of Insights Into the Importance of Hydrogen Bonding in the Gamma- Phosphate Binding Pocket of Myosin: Structural and Functional Studies of SER236 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Insights Into the Importance of Hydrogen Bonding in the Gamma- Phosphate Binding Pocket of Myosin: Structural and Functional Studies of SER236 (pdb code 3myh). 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 Insights Into the Importance of Hydrogen Bonding in the Gamma- Phosphate Binding Pocket of Myosin: Structural and Functional Studies of SER236, PDB code: 3myh:

Vanadium binding site 1 out of 1 in 3myh

Go back to Vanadium Binding Sites List in 3myh
Vanadium binding site 1 out of 1 in the Insights Into the Importance of Hydrogen Bonding in the Gamma- Phosphate Binding Pocket of Myosin: Structural and Functional Studies of SER236


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Insights Into the Importance of Hydrogen Bonding in the Gamma- Phosphate Binding Pocket of Myosin: Structural and Functional Studies of SER236 within 5.0Å range:
probe atom residue distance (Å) B Occ
X:V998

b:13.5
occ:1.00
V X:VO4998 0.0 13.5 1.0
O1 X:VO4998 1.8 14.2 1.0
O2 X:VO4998 1.9 15.1 1.0
O3 X:VO4998 1.9 13.4 1.0
O4 X:VO4998 2.0 16.6 1.0
O3B X:ADP999 2.1 15.2 1.0
PB X:ADP999 3.3 12.1 1.0
MG X:MG997 3.5 12.0 1.0
O1B X:ADP999 3.6 12.4 1.0
N X:SER237 3.8 14.2 1.0
OG X:SER181 3.8 15.2 1.0
ND2 X:ASN233 3.9 16.1 1.0
N X:GLY182 3.9 13.0 1.0
CA X:SER181 4.0 11.7 1.0
O X:HOH780 4.0 12.4 1.0
O X:HOH792 4.0 15.0 1.0
NZ X:LYS185 4.0 13.6 1.0
CA X:ALA236 4.1 13.3 1.0
N X:GLY457 4.2 11.5 1.0
O2B X:ADP999 4.2 16.0 1.0
O X:HOH787 4.2 14.4 1.0
CB X:SER181 4.3 11.9 1.0
CB X:SER237 4.4 12.9 1.0
O X:SER237 4.4 12.2 1.0
O3A X:ADP999 4.4 13.2 1.0
CB X:ALA236 4.4 9.4 1.0
C X:SER181 4.4 12.5 1.0
C X:ALA236 4.5 14.2 1.0
OG X:SER237 4.6 13.4 1.0
CE X:LYS185 4.6 11.1 1.0
CA X:SER237 4.7 12.6 1.0
CA X:SER456 4.8 13.9 1.0
CG X:ASN233 4.9 14.9 1.0
CA X:GLY457 4.9 11.2 1.0
CB X:ASN233 5.0 14.3 1.0

Reference:

J.J.Frye, V.A.Klenchin, C.R.Bagshaw, I.Rayment. Insights Into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Serine 236 Biochemistry V. 49 4897 2010.
ISSN: ISSN 0006-2960
PubMed: 20459085
DOI: 10.1021/BI1001344
Page generated: Thu Oct 29 07:05:06 2020

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