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Sodium in PDB 4ka7: Structure of Organellar Oligopeptidase (E572Q) in Complex with An Endogenous Substrate

Protein crystallography data

The structure of Structure of Organellar Oligopeptidase (E572Q) in Complex with An Endogenous Substrate, PDB code: 4ka7 was solved by R.P.-A.Berntsson, B.Kmiec, P.F.Teixeira, L.M.Svensson, A.Bakali, E.Glaser, P.Stenmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.65 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.466, 100.771, 132.484, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 19.9

Other elements in 4ka7:

The structure of Structure of Organellar Oligopeptidase (E572Q) in Complex with An Endogenous Substrate also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Zinc (Zn) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Organellar Oligopeptidase (E572Q) in Complex with An Endogenous Substrate (pdb code 4ka7). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of Organellar Oligopeptidase (E572Q) in Complex with An Endogenous Substrate, PDB code: 4ka7:

Sodium binding site 1 out of 1 in 4ka7

Go back to Sodium Binding Sites List in 4ka7
Sodium binding site 1 out of 1 in the Structure of Organellar Oligopeptidase (E572Q) in Complex with An Endogenous Substrate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Organellar Oligopeptidase (E572Q) in Complex with An Endogenous Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na805

b:21.1
occ:1.00
O A:HOH945 2.3 24.2 1.0
O A:MET379 2.3 20.2 1.0
O A:ALA384 2.4 18.9 1.0
O A:LYS382 2.4 17.7 1.0
O A:HOH1043 2.5 29.6 1.0
O A:HOH999 2.5 29.2 1.0
C A:LYS382 3.4 18.5 1.0
C A:MET379 3.4 20.1 1.0
C A:ALA384 3.5 18.8 1.0
O A:HOH1017 3.6 32.6 1.0
C A:MET383 4.0 19.1 1.0
O A:MET383 4.0 19.3 1.0
N A:LYS382 4.0 19.7 1.0
CA A:LYS382 4.2 19.1 1.0
N A:ALA384 4.2 18.3 1.0
CB A:MET379 4.2 20.8 1.0
CA A:MET379 4.2 20.3 1.0
N A:MET383 4.4 18.4 1.0
N A:ALA380 4.4 20.0 1.0
N A:THR385 4.5 19.6 1.0
CA A:ALA384 4.5 18.2 1.0
CB A:LYS382 4.5 19.6 1.0
C A:ALA380 4.5 21.4 1.0
O A:ALA380 4.5 20.9 1.0
CG2 A:THR385 4.5 21.5 1.0
O A:HOH1215 4.5 40.1 1.0
CA A:ALA380 4.6 20.7 1.0
CA A:MET383 4.6 19.1 1.0
CA A:THR385 4.6 20.6 1.0

Reference:

B.Kmiec, P.F.Teixeira, R.P.-A.Berntsson, M.W.Murcha, R.M.M.Branca, J.Radomiljac, J.Regberg, L.M.Svensson, A.Bakali, U.Langel, J.Lehtio, J.Whelan, P.Stenmark, E.Glaser. Organellar Oligopeptidase (Oop) Provides A Complementary Pathway For Targeting Peptide Degradation in Mitochondria and Chloroplasts Proc.Natl.Acad.Sci.Usa 2013.
ISSN: ESSN 1091-6490
Page generated: Mon Oct 7 16:26:53 2024

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