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Sodium in PDB 5bpm: Crystal Structure of Unhydrolyzed Atp Bound Human HSP70 Nbd Double Mutant E268Q+R272K.

Protein crystallography data

The structure of Crystal Structure of Unhydrolyzed Atp Bound Human HSP70 Nbd Double Mutant E268Q+R272K., PDB code: 5bpm was solved by D.Narayanan, R.A.Engh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.08 / 1.83
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.466, 64.278, 144.860, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 22.8

Other elements in 5bpm:

The structure of Crystal Structure of Unhydrolyzed Atp Bound Human HSP70 Nbd Double Mutant E268Q+R272K. also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Unhydrolyzed Atp Bound Human HSP70 Nbd Double Mutant E268Q+R272K. (pdb code 5bpm). 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 Crystal Structure of Unhydrolyzed Atp Bound Human HSP70 Nbd Double Mutant E268Q+R272K., PDB code: 5bpm:

Sodium binding site 1 out of 1 in 5bpm

Go back to Sodium Binding Sites List in 5bpm
Sodium binding site 1 out of 1 in the Crystal Structure of Unhydrolyzed Atp Bound Human HSP70 Nbd Double Mutant E268Q+R272K.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Unhydrolyzed Atp Bound Human HSP70 Nbd Double Mutant E268Q+R272K. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na404

b:13.9
occ:1.00
O1B A:ATP401 2.2 14.1 1.0
O A:TYR15 2.3 11.5 1.0
O A:HOH614 2.3 11.5 1.0
OD2 A:ASP10 2.4 13.6 1.0
CG A:ASP10 3.2 9.9 1.0
HA3 A:GLY12 3.2 12.9 1.0
PB A:ATP401 3.4 12.7 1.0
C A:TYR15 3.4 10.8 1.0
HA A:SER16 3.4 12.5 1.0
OD1 A:ASP10 3.6 9.4 1.0
O A:HOH552 3.6 15.7 1.0
O A:HOH591 3.8 12.5 1.0
O2A A:ATP401 3.8 14.6 1.0
O2B A:ATP401 3.9 12.3 1.0
O3A A:ATP401 3.9 14.1 1.0
HB2 A:TYR15 3.9 16.4 1.0
CA A:GLY12 4.0 10.8 1.0
H A:GLY12 4.0 14.7 1.0
CA A:SER16 4.1 10.4 1.0
HB3 A:ASP10 4.1 12.9 1.0
N A:SER16 4.1 13.6 1.0
HA2 A:GLY12 4.1 12.9 1.0
PA A:ATP401 4.2 12.9 1.0
H A:TYR15 4.2 11.1 1.0
N A:GLY12 4.3 12.2 1.0
CB A:ASP10 4.3 10.7 1.0
HB3 A:TYR15 4.3 16.4 1.0
HB2 A:CYS17 4.3 14.7 1.0
CA A:TYR15 4.4 8.8 1.0
O A:ASP10 4.4 11.9 1.0
O1A A:ATP401 4.4 15.6 1.0
CB A:TYR15 4.4 13.7 1.0
O A:HOH624 4.4 12.3 1.0
O A:ASP366 4.5 11.2 1.0
C A:SER16 4.5 10.7 1.0
H A:CYS17 4.6 13.0 1.0
HB3 A:CYS17 4.6 14.7 1.0
N A:CYS17 4.7 10.9 1.0
O3B A:ATP401 4.7 9.4 1.0
N A:TYR15 4.7 9.2 1.0
C A:ASP10 4.9 8.4 1.0
O A:HOH580 4.9 14.5 1.0
HB2 A:ASP366 4.9 12.3 1.0
H A:SER16 4.9 16.3 1.0
HB2 A:ASP10 4.9 12.9 1.0
CB A:CYS17 4.9 12.2 1.0

Reference:

D.Narayanan, A.Pflug, T.Christopeit, P.Kyomuhendo, R.A.Engh. Nucleotide Binding to Variants of the HSP70-Nbd. To Be Published.
Page generated: Tue Dec 15 10:29:41 2020

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