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Potassium in PDB 1sds: Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna

Protein crystallography data

The structure of Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna, PDB code: 1sds was solved by T.Hamma, A.Ferre-D'amare, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.48 / 1.80
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 106.970, 141.300, 162.870, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 22.5

Other elements in 1sds:

The structure of Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna also contains other interesting chemical elements:

Calcium (Ca) 10 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna (pdb code 1sds). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna, PDB code: 1sds:

Potassium binding site 1 out of 1 in 1sds

Go back to Potassium Binding Sites List in 1sds
Potassium binding site 1 out of 1 in the Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna within 5.0Å range:
probe atom residue distance (Å) B Occ
E:K761

b:53.8
occ:1.00
N2 E:G213 3.4 24.5 1.0
O2' E:G214 4.1 26.4 1.0
O4' E:G214 4.2 27.7 1.0
C1' E:G214 4.2 25.2 1.0
C2 E:G213 4.4 23.9 1.0
N3 E:G213 4.4 24.4 1.0
C2' E:G214 4.8 24.1 1.0
C4' E:G214 4.8 25.1 1.0
O E:HOH1118 4.9 41.8 1.0

Reference:

T.Hamma, A.Ferre-D'amare. Structure of Protein L7AE Bound to A K-Turn Derived From An Archaeal Box H/Aca Srna at 1.8 A Resolution. Structure V. 12 893 2004.
ISSN: ISSN 0969-2126
PubMed: 15130481
DOI: 10.1016/J.STR.2004.03.015
Page generated: Mon Aug 12 05:22:34 2024

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