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Magnesium in PDB 1nga: Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment

Enzymatic activity of Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment

All present enzymatic activity of Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment:
3.6.1.3;

Protein crystallography data

The structure of Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment, PDB code: 1nga was solved by K.M.Flaherty, S.M.Wilbanks, C.Deluca-Flaherty, D.B.Mckay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.18
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 145.300, 65.000, 46.900, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment (pdb code 1nga). 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 Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment, PDB code: 1nga:

Magnesium binding site 1 out of 1 in 1nga

Go back to Magnesium Binding Sites List in 1nga
Magnesium binding site 1 out of 1 in the Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity, II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg487

b:12.8
occ:0.88
 O A:HOH663 2.0 2.0 0.6
O A:HOH659 2.0 2.0 0.8
O A:HOH586 2.1 36.2 1.0
O A:HOH661 2.2 27.0 1.0
O2B A:ADP486 2.2 9.4 1.0
O A:HOH662 2.6 28.9 1.0
PB A:ADP486 3.4 11.3 1.0
O A:HOH502 3.5 2.0 1.0
O1B A:ADP486 3.8 9.7 1.0
OD2 A:ASP199 4.0 7.7 1.0
O1A A:ADP486 4.0 9.7 1.0
OD1 A:ASP199 4.1 7.8 1.0
O A:HOH596 4.3 3.2 0.7
OD1 A:ASP10 4.3 8.7 1.0
OD2 A:ASP10 4.3 7.4 1.0
O A:HOH601 4.4 32.9 1.0
O3A A:ADP486 4.4 9.2 1.0
O A:HOH660 4.5 7.1 1.0
CG A:ASP199 4.5 8.1 1.0
O A:HOH579 4.6 8.8 1.0
O3B A:ADP486 4.6 14.6 1.0
CG A:ASP10 4.7 3.5 1.0
CG2 A:VAL369 4.9 2.0 1.0
PA A:ADP486 4.9 6.8 1.0
CA A:GLY12 5.0 5.8 1.0

Reference:

K.M.Flaherty, S.M.Wilbanks, C.Deluca-Flaherty, D.B.Mckay. Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein Atp Hydrolytic Activity. II. Structure of the Active Site with Adp or Atp Bound to Wild Type and Mutant Atpase Fragment. J.Biol.Chem. V. 269 12899 1994.
ISSN: ISSN 0021-9258
PubMed: 8175707
Page generated: Tue Aug 13 09:51:21 2024

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