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Magnesium in PDB 1atr: Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis

Enzymatic activity of Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis

All present enzymatic activity of Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis:
3.6.1.3;

Protein crystallography data

The structure of Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis, PDB code: 1atr was solved by M.C.O'brien, D.B.Mckay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.34
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 (%) 21.8 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis (pdb code 1atr). 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 Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis, PDB code: 1atr:

Magnesium binding site 1 out of 1 in 1atr

Go back to Magnesium Binding Sites List in 1atr
Magnesium binding site 1 out of 1 in the Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg487

b:25.9
occ:1.00
 O A:HOH610 2.0 39.1 1.0
O A:HOH612 2.0 37.7 1.0
O A:HOH609 2.1 29.2 1.0
O1A A:ADP486 2.3 11.4 1.0
O2B A:ADP486 2.3 17.3 1.0
O A:HOH611 2.4 20.5 1.0
PB A:ADP486 3.4 15.9 1.0
PA A:ADP486 3.5 11.8 1.0
O2 A:PO4488 3.7 80.2 1.0
O3A A:ADP486 3.7 14.4 1.0
OD2 A:ASP10 3.8 12.1 1.0
O A:HOH614 4.0 60.5 1.0
O3B A:ADP486 4.1 18.7 1.0
O A:HOH506 4.2 20.7 1.0
CA A:GLY338 4.3 11.0 1.0
O3 A:PO4488 4.3 79.1 1.0
O2A A:ADP486 4.3 10.4 1.0
P A:PO4488 4.4 79.3 1.0
O4 A:PO4488 4.4 79.2 1.0
OD1 A:ASP199 4.5 8.4 1.0
O1B A:ADP486 4.6 16.6 1.0
OD1 A:ASP10 4.6 11.1 1.0
O5' A:ADP486 4.6 7.5 1.0
CG A:ASP10 4.7 8.2 1.0
O A:HOH613 4.7 58.5 1.0
N A:GLY338 4.8 11.7 1.0
OD2 A:ASP199 4.9 9.2 1.0
O A:ASP366 5.0 13.2 1.0

Reference:

M.C.O'brien, D.B.Mckay. Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site, But Is Not Essential For Atp Hydrolysis. J.Biol.Chem. V. 268 24323 1993.
ISSN: ISSN 0021-9258
PubMed: 8226982
Page generated: Tue Aug 13 02:08:21 2024

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