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Sodium in PDB 1ba1: Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys

Enzymatic activity of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys

All present enzymatic activity of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys:
3.6.1.3;

Protein crystallography data

The structure of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys, PDB code: 1ba1 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) 6.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 143.800, 64.100, 46.100, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 24.4

Other elements in 1ba1:

The structure of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys 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 Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys (pdb code 1ba1). 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 Mutant with Cys 17 Replaced By Lys, PDB code: 1ba1:

Sodium binding site 1 out of 1 in 1ba1

Go back to Sodium Binding Sites List in 1ba1
Sodium binding site 1 out of 1 in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys


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 Mutant with Cys 17 Replaced By Lys within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na491

b:31.3
occ:1.00
 O A:HOH564 2.9 39.0 0.0
OG1 A:THR204 3.1 13.6 1.0
OD2 A:ASP206 3.1 18.0 1.0
OD1 A:ASP199 3.1 7.9 1.0
O A:THR204 3.3 10.4 1.0
O A:ASP199 3.4 7.2 1.0
CG A:ASP199 3.4 9.0 1.0
N A:GLY201 3.7 8.1 1.0
OD2 A:ASP199 3.8 9.9 1.0
C A:THR204 3.8 10.1 1.0
O A:HOH560 3.9 11.0 1.0
C A:ASP199 4.0 5.1 1.0
CB A:ASP199 4.0 7.2 1.0
CG A:ASP206 4.0 17.2 1.0
N A:ASP206 4.1 8.2 1.0
CB A:THR204 4.1 11.6 1.0
O A:HOH509 4.1 19.0 1.0
CA A:GLY201 4.2 8.1 1.0
O A:HOH561 4.3 10.1 1.0
N A:PHE205 4.3 9.2 1.0
CB A:ASP206 4.3 12.6 1.0
O3B A:ADP486 4.4 14.2 1.0
CA A:PHE205 4.5 8.9 1.0
MG A:MG487 4.5 16.9 1.0
O A:HOH551 4.5 14.1 1.0
CA A:THR204 4.5 10.1 1.0
C A:PHE205 4.6 8.9 1.0
N A:LEU200 4.6 5.8 1.0
C A:LEU200 4.6 8.0 1.0
CA A:ASP199 4.7 6.2 1.0
O A:HOH579 4.7 25.7 1.0
CA A:LEU200 4.8 6.5 1.0
CA A:ASP206 4.9 9.3 1.0
O A:HOH819 4.9 19.9 1.0

Reference:

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
Page generated: Sun Oct 6 17:54:40 2024

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