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Magnesium 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:

Chlorine (Cl) 2 atoms
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was determined in the Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal Mutant with Cys 17 Replaced By Lys, PDB code: 1ba1:

Magnesium binding site 1 out of 1 in 1ba1

Go back to Magnesium Binding Sites List in 1ba1
Magnesium 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 Magnesium with other atoms in the Mg 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:Mg487

b:16.9
occ:1.00
 O A:HOH564 1.9 39.0 0.0
O A:HOH560 2.1 11.0 1.0
O A:HOH562 2.1 8.4 1.0
O A:HOH563 2.1 12.0 1.0
O1B A:ADP486 2.2 10.7 1.0
O A:HOH561 2.2 10.1 1.0
PB A:ADP486 3.2 11.6 1.0
O3B A:ADP486 3.4 14.2 1.0
O A:HOH579 3.8 25.7 1.0
O1A A:ADP486 3.9 7.0 1.0
OD2 A:ASP10 4.1 8.8 1.0
OD2 A:ASP199 4.1 9.9 1.0
O3A A:ADP486 4.2 10.0 1.0
OD1 A:ASP199 4.2 7.9 1.0
OE1 A:GLU175 4.3 14.1 1.0
OD1 A:ASP10 4.3 8.1 1.0
NZ A:LYS17 4.4 5.8 1.0
O2B A:ADP486 4.4 11.5 1.0
NA A:NA491 4.5 31.3 1.0
PA A:ADP486 4.6 8.5 1.0
CG A:ASP199 4.6 9.0 1.0
CG A:ASP10 4.6 9.5 1.0
O A:HOH573 4.8 6.3 1.0
CA A:GLY12 4.9 7.5 1.0
CD A:GLU175 4.9 12.3 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: Mon Dec 14 03:48:51 2020

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