Sodium in PDB 1ba0: Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3

All present enzymatic activity of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3:
3.6.1.3;

The structure of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3, PDB code: 1ba0 was solved by S.M.Wilbanks, D.B.Mckay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	143.300, 63.800, 46.500, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 27.5

The structure of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 also contains other interesting chemical elements:

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

The binding sites of Sodium atom in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 (pdb code 1ba0). 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 Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3, PDB code: 1ba0:

Sodium binding site 1 out of 1 in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na490 b:10.3 occ:1.00 O A:HOH558 2.3 6.4 1.0 O2B A:ADP486 2.4 12.5 1.0 O A:TYR15 2.4 8.1 1.0 OD2 A:ASP10 2.5 11.0 1.0 O A:HOH563 2.8 7.9 1.0 O3A A:ADP486 3.3 12.2 1.0 PB A:ADP486 3.3 10.2 1.0 CG A:ASP10 3.3 8.9 1.0 O A:HOH562 3.4 9.2 1.0 MG A:MG487 3.4 11.8 1.0 OD1 A:ASP10 3.5 10.5 1.0 C A:TYR15 3.5 9.4 1.0 O1A A:ADP486 3.8 9.5 1.0 PA A:ADP486 3.9 10.1 1.0 O3B A:ADP486 3.9 13.9 1.0 O2A A:ADP486 4.0 12.5 1.0 CA A:GLY12 4.0 8.1 1.0 N A:SER16 4.4 8.4 1.0 O A:ASP366 4.4 13.4 1.0 O A:HOH1058 4.4 12.8 1.0 CA A:TYR15 4.4 8.6 1.0 CA A:SER16 4.5 8.0 1.0 N A:GLY12 4.5 6.6 1.0 CB A:TYR15 4.5 8.1 1.0 O1B A:ADP486 4.6 13.5 1.0 N A:TYR15 4.6 9.8 1.0 CB A:ASP10 4.7 9.2 1.0 O A:HOH560 4.7 8.7 1.0 O A:HOH573 4.8 6.1 1.0 C A:SER16 4.8 8.3 1.0 O3 A:PO4488 4.9 13.9 1.0 O A:ASP10 5.0 8.3 1.0

S.M.Wilbanks, D.B.Mckay. Structural Replacement of Active Site Monovalent Cations By the Epsilon-Amino Group of Lysine in the Atpase Fragment of Bovine HSC70. Biochemistry V. 37 7456 1998.
ISSN: ISSN 0006-2960
PubMed: 9585559
DOI: 10.1021/BI973046M