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Potassium in PDB 4o8p: Crystal Structure of STHARAF62A, A GH62 Family Alpha-L- Arabinofuranosidase From Streptomyces Thermoviolaceus, Bound to Xylotetraose

Protein crystallography data

The structure of Crystal Structure of STHARAF62A, A GH62 Family Alpha-L- Arabinofuranosidase From Streptomyces Thermoviolaceus, Bound to Xylotetraose, PDB code: 4o8p was solved by P.J.Stogios, W.Wang, X.Xu, H.Cui, E.Master, A.Savchenko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.68 / 1.56
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.491, 64.637, 121.303, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 15.3

Other elements in 4o8p:

The structure of Crystal Structure of STHARAF62A, A GH62 Family Alpha-L- Arabinofuranosidase From Streptomyces Thermoviolaceus, Bound to Xylotetraose also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of STHARAF62A, A GH62 Family Alpha-L- Arabinofuranosidase From Streptomyces Thermoviolaceus, Bound to Xylotetraose (pdb code 4o8p). 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 Crystal Structure of STHARAF62A, A GH62 Family Alpha-L- Arabinofuranosidase From Streptomyces Thermoviolaceus, Bound to Xylotetraose, PDB code: 4o8p:

Potassium binding site 1 out of 1 in 4o8p

Go back to Potassium Binding Sites List in 4o8p
Potassium binding site 1 out of 1 in the Crystal Structure of STHARAF62A, A GH62 Family Alpha-L- Arabinofuranosidase From Streptomyces Thermoviolaceus, Bound to Xylotetraose


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of STHARAF62A, A GH62 Family Alpha-L- Arabinofuranosidase From Streptomyces Thermoviolaceus, Bound to Xylotetraose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K408

b:11.5
occ:0.71
O A:HOH556 2.6 18.3 1.0
O A:HOH532 2.8 16.7 1.0
O A:HOH524 2.8 12.9 1.0
O3B A:XYP406 2.8 13.8 1.0
O A:HOH664 2.8 30.3 1.0
O A:HOH552 3.0 15.1 1.0
O A:HOH961 3.6 51.4 1.0
OH A:TYR349 3.6 13.8 1.0
C3B A:XYP406 3.8 9.7 1.0
NZ A:LYS87 3.9 12.2 1.0
OE2 A:GLU248 4.1 11.9 1.0
O A:HOH512 4.2 11.8 1.0
OE1 A:GLU248 4.3 14.4 1.0
OD1 A:ASP88 4.4 12.1 1.0
CD A:GLU248 4.4 13.7 1.0
CE2 A:TYR349 4.4 9.3 1.0
OD2 A:ASP88 4.5 10.7 1.0
O2B A:XYP406 4.5 12.1 1.0
CZ A:TYR349 4.5 10.1 1.0
CD1 A:ILE195 4.6 24.4 1.0
O4B A:XYP406 4.6 12.4 1.0
OD1 A:ASP196 4.7 11.2 1.0
C2B A:XYP406 4.7 11.6 1.0
C4B A:XYP406 4.8 13.6 1.0
CE A:LYS87 4.8 8.8 1.0
OD2 A:ASP196 4.8 12.2 1.0
CG A:ASP88 4.9 11.2 1.0
ND1 A:HIS315 5.0 8.9 1.0

Reference:

W.Wang, G.Mai-Gisondi, P.J.Stogios, A.Kaur, X.Xu, H.Cui, O.Turunen, A.Savchenko, E.R.Master. Biochemical and Structural Characterization of A Thermostable Family GH62 Alpha-L-Arabinofuranosidase From Streptomyces Thermoviolaceus to Elucidate the Molecular Basis For Activity Towards Arabinoxylan. Appl.Environ.Microbiol. 2014.
ISSN: ESSN 1098-5336
PubMed: 24951792
DOI: 10.1128/AEM.00685-14
Page generated: Mon Aug 12 11:41:58 2024

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