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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1ba0:

The structure of Heat-Shock Cognate 70KD Protein 44KD Atpase N-Terminal 1NGE 3 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 1NGE 3 (pdb code 1ba0). 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 1NGE 3, PDB code: 1ba0:

Magnesium binding site 1 out of 1 in 1ba0

Go back to Magnesium Binding Sites List in 1ba0
Magnesium 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 Magnesium with other atoms in the Mg 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:Mg487

b:11.8
occ:1.00
O A:HOH561 2.0 13.4 1.0
O A:HOH562 2.1 9.2 1.0
O2B A:ADP486 2.1 12.5 1.0
O2 A:PO4488 2.1 11.8 1.0
O A:HOH563 2.2 7.9 1.0
O A:HOH560 2.2 8.7 1.0
PB A:ADP486 3.3 10.2 1.0
P A:PO4488 3.3 13.2 1.0
NA A:NA490 3.4 10.3 1.0
O3 A:PO4488 3.4 13.9 1.0
O1B A:ADP486 3.6 13.5 1.0
O1A A:ADP486 4.0 9.5 1.0
O1 A:PO4488 4.1 15.5 1.0
NZ A:LYS206 4.1 9.8 1.0
OD2 A:ASP199 4.2 8.7 1.0
OE1 A:GLU175 4.3 11.7 1.0
O3A A:ADP486 4.3 12.2 1.0
OD1 A:ASP199 4.3 6.8 1.0
O3B A:ADP486 4.4 13.9 1.0
OD1 A:ASP10 4.4 10.5 1.0
OD2 A:ASP10 4.4 11.0 1.0
O4 A:PO4488 4.4 12.4 1.0
CG A:ASP199 4.7 9.9 1.0
CE A:LYS206 4.7 9.4 1.0
O A:HOH573 4.8 6.1 1.0
O A:HOH545 4.8 7.4 1.0
CG A:ASP10 4.8 8.9 1.0
PA A:ADP486 4.8 10.1 1.0
CD A:GLU175 4.8 12.4 1.0
CG2 A:VAL369 5.0 6.1 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 03:47:17 2020

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