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Strontium in PDB 5lt0: Nucleotide-Free Kinesin-1 Motor Domain, P212121 Crystal Form

Protein crystallography data

The structure of Nucleotide-Free Kinesin-1 Motor Domain, P212121 Crystal Form, PDB code: 5lt0 was solved by L.Cao, B.Gigant, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.94 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.029, 68.058, 112.378, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 21.5

Strontium Binding Sites:

The binding sites of Strontium atom in the Nucleotide-Free Kinesin-1 Motor Domain, P212121 Crystal Form (pdb code 5lt0). This binding sites where shown within 5.0 Angstroms radius around Strontium atom.
In total only one binding site of Strontium was determined in the Nucleotide-Free Kinesin-1 Motor Domain, P212121 Crystal Form, PDB code: 5lt0:

Strontium binding site 1 out of 1 in 5lt0

Go back to Strontium Binding Sites List in 5lt0
Strontium binding site 1 out of 1 in the Nucleotide-Free Kinesin-1 Motor Domain, P212121 Crystal Form


Mono view


Stereo pair view

A full contact list of Strontium with other atoms in the Sr binding site number 1 of Nucleotide-Free Kinesin-1 Motor Domain, P212121 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sr402

b:80.8
occ:1.00
ND2 A:ASN255 3.1 57.5 1.0
OD1 A:ASN255 3.5 41.9 1.0
O A:HOH581 3.6 42.5 1.0
NE2 A:HIS205 3.6 28.2 1.0
OG A:SER257 3.6 34.8 1.0
N A:ASP140 3.6 38.5 1.0
CG A:ASN255 3.6 54.8 1.0
N A:SER257 3.9 25.6 1.0
N A:LEU139 4.1 39.3 1.0
O A:HOH623 4.1 50.4 1.0
CB A:SER257 4.1 30.1 1.0
CD2 A:HIS205 4.1 26.4 1.0
N A:LYS256 4.3 36.9 1.0
CA A:LEU139 4.3 41.7 1.0
CA A:ASP140 4.4 52.2 1.0
CB A:LYS256 4.4 36.6 1.0
C A:LEU139 4.4 37.3 1.0
CG2 A:ILE137 4.5 27.9 1.0
CA A:SER257 4.6 32.3 1.0
CA A:LYS256 4.7 32.8 1.0
C A:LYS256 4.8 33.1 1.0
CE1 A:HIS205 4.8 28.3 1.0
CB A:ASP140 4.8 52.4 1.0
C A:TYR138 5.0 39.0 1.0

Reference:

L.Cao, S.Cantos-Fernandes, B.Gigant. The Structural Switch of Nucleotide-Free Kinesin. Sci Rep V. 7 42558 2017.
ISSN: ESSN 2045-2322
PubMed: 28195215
DOI: 10.1038/SREP42558
Page generated: Fri Oct 11 06:24:47 2024

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