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Magnesium in PDB 4l79: Crystal Structure of Nucleotide-Free Myosin 1B Residues 1-728 with Bound Calmodulin

Protein crystallography data

The structure of Crystal Structure of Nucleotide-Free Myosin 1B Residues 1-728 with Bound Calmodulin, PDB code: 4l79 was solved by H.Shuman, A.Zwolak, R.Dominguez, E.M.Ostap, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.21 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 114.184, 45.090, 115.547, 90.00, 117.18, 90.00
R / Rfree (%) 18.9 / 24.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Nucleotide-Free Myosin 1B Residues 1-728 with Bound Calmodulin (pdb code 4l79). 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 Crystal Structure of Nucleotide-Free Myosin 1B Residues 1-728 with Bound Calmodulin, PDB code: 4l79:

Magnesium binding site 1 out of 1 in 4l79

Go back to Magnesium Binding Sites List in 4l79
Magnesium binding site 1 out of 1 in the Crystal Structure of Nucleotide-Free Myosin 1B Residues 1-728 with Bound Calmodulin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Nucleotide-Free Myosin 1B Residues 1-728 with Bound Calmodulin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg801

b:32.6
occ:1.00
OD1 A:ASN563 2.3 26.9 1.0
O A:HOH1010 2.5 34.4 1.0
O A:GLU556 2.5 26.2 1.0
O A:LYS561 2.6 29.8 1.0
O A:ASN558 2.7 24.1 1.0
O A:HOH1066 2.8 36.0 1.0
CG A:ASN563 3.3 29.3 1.0
C A:GLU556 3.6 25.3 1.0
C A:ASN558 3.6 21.4 1.0
O A:HOH955 3.7 28.2 1.0
C A:LYS561 3.7 22.0 1.0
ND2 A:ASN563 3.9 33.4 1.0
C A:GLY557 3.9 18.5 1.0
O A:HOH1185 4.0 34.2 1.0
O A:GLY557 4.1 19.3 1.0
CA A:GLY557 4.2 21.6 1.0
N A:ASN558 4.2 22.2 1.0
N A:ASN563 4.2 22.1 1.0
N A:PRO559 4.3 19.9 1.0
CA A:PRO559 4.3 27.8 1.0
N A:GLY557 4.4 25.5 1.0
CA A:LYS561 4.5 22.4 1.0
CB A:LYS561 4.5 25.1 1.0
N A:LYS561 4.5 21.2 1.0
C A:VAL562 4.5 24.2 1.0
CB A:ASN563 4.5 28.0 1.0
CA A:ASN563 4.5 27.5 1.0
CA A:ASN558 4.6 20.7 1.0
O A:HOH916 4.6 26.5 1.0
CA A:GLU556 4.6 21.5 1.0
C A:PRO559 4.6 27.9 1.0
O A:HOH1322 4.7 45.5 1.0
O A:PRO559 4.7 24.7 1.0
N A:VAL562 4.7 27.0 1.0
OE1 A:GLN540 4.8 40.7 1.0
CA A:VAL562 4.8 24.6 1.0
O A:VAL562 5.0 19.5 1.0

Reference:

H.Shuman, M.J.Greenberg, A.Zwolak, T.Lin, C.V.Sindelar, R.Dominguez, E.M.Ostap. A Vertebrate Myosin-I Structure Reveals Unique Insights Into Myosin Mechanochemical Tuning. Proc.Natl.Acad.Sci.Usa V. 111 2116 2014.
ISSN: ISSN 0027-8424
PubMed: 24469830
DOI: 10.1073/PNAS.1321022111
Page generated: Sat Aug 17 04:27:03 2024

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