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Magnesium in PDB 3myl: 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: 3myl 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) 29.69 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 104.045, 180.779, 53.890, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium 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 3myl). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium 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: 3myl:

Magnesium binding site 1 out of 1 in 3myl

Go back to Magnesium Binding Sites List in 3myl
Magnesium 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 Magnesium with other atoms in the Mg 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:Mg998

b:10.2
occ:1.00
O X:HOH1129 2.0 10.8 1.0
O4 X:POP999 2.1 9.2 1.0
OG1 X:THR186 2.1 12.0 1.0
O1 X:POP999 2.1 7.7 1.0
OG X:SER237 2.1 9.0 1.0
O X:HOH1111 2.2 8.1 1.0
CB X:THR186 3.1 10.1 1.0
CB X:SER237 3.1 10.3 1.0
P2 X:POP999 3.2 8.5 1.0
P1 X:POP999 3.3 9.8 1.0
O X:POP999 3.5 9.5 1.0
N X:SER237 3.8 10.7 1.0
N X:THR186 3.9 8.2 1.0
O6 X:POP999 3.9 9.2 1.0
CA X:THR186 4.0 9.8 1.0
CA X:SER237 4.1 10.7 1.0
CG2 X:THR186 4.1 11.0 1.0
OD1 X:ASP454 4.2 10.7 1.0
OD2 X:ASP454 4.2 15.7 1.0
O3 X:POP999 4.2 8.8 1.0
O2 X:POP999 4.3 8.3 1.0
O X:HOH1139 4.4 12.4 1.0
O5 X:POP999 4.4 8.9 1.0
O X:HOH1120 4.5 16.0 1.0
O X:HOH1117 4.5 18.0 1.0
O X:HOH1781 4.6 20.7 1.0
CG X:ASP454 4.7 13.6 1.0
O X:ASN235 4.7 12.7 1.0
O X:HOH1118 4.8 11.7 1.0
CE X:LYS185 4.9 11.0 1.0
ND2 X:ASN233 4.9 10.5 1.0
C X:ALA236 4.9 11.3 1.0
CB X:LYS185 4.9 8.1 1.0
C X:LYS185 5.0 9.2 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: Mon Dec 14 08:27:19 2020

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