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Chlorine in PDB 1hpm: How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site

Enzymatic activity of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site

All present enzymatic activity of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site:
3.6.1.3;

Protein crystallography data

The structure of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site, PDB code: 1hpm 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) N/A / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 143.900, 63.700, 46.200, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / n/a

Other elements in 1hpm:

The structure of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Potassium (K) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site (pdb code 1hpm). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site, PDB code: 1hpm:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1hpm

Go back to Chlorine Binding Sites List in 1hpm
Chlorine binding site 1 out of 2 in the How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl828

b:11.4
occ:1.00
O A:HOH612 3.3 6.8 1.0
NZ A:LYS126 3.3 10.0 1.0
N A:ASP32 3.3 11.5 1.0
NE2 A:GLN33 3.4 10.3 1.0
CB A:ASN31 3.4 8.0 1.0
CB A:ASP32 3.5 13.9 1.0
CG A:ASP32 3.6 17.8 1.0
CD A:LYS126 3.8 9.6 1.0
O A:HOH830 3.8 22.8 1.0
CG A:ASN31 3.9 6.6 1.0
OD1 A:ASP32 3.9 18.8 1.0
OD2 A:ASP32 4.0 18.9 1.0
CE A:LYS126 4.0 9.5 1.0
CA A:ASP32 4.0 13.0 1.0
OE1 A:GLN33 4.1 14.6 1.0
CD A:GLN33 4.2 12.1 1.0
O A:HOH831 4.2 16.4 1.0
ND2 A:ASN31 4.2 6.9 1.0
CG1 A:ILE130 4.2 9.4 1.0
C A:ASN31 4.3 10.8 1.0
O A:HOH774 4.3 10.7 1.0
CA A:ASN31 4.3 9.8 1.0
CD1 A:ILE130 4.3 9.8 1.0
OD1 A:ASN31 4.4 6.4 1.0
O A:HOH771 4.6 16.4 1.0
N A:GLN33 4.7 12.1 1.0
C A:ASP32 4.9 12.9 1.0
O A:HOH962 5.0 30.8 1.0
CG A:LYS126 5.0 10.2 1.0

Chlorine binding site 2 out of 2 in 1hpm

Go back to Chlorine Binding Sites List in 1hpm
Chlorine binding site 2 out of 2 in the How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl523

b:10.0
occ:1.00
O A:HOH537 2.9 8.8 1.0
NZ A:LYS345 3.1 15.4 1.0
NZ A:LYS348 3.3 9.8 1.0
CE A:LYS345 3.5 13.0 1.0
NH2 A:ARG311 4.0 22.5 1.0
CD A:LYS348 4.0 11.4 1.0
CD2 A:LEU349 4.1 9.6 1.0
CE A:LYS348 4.1 11.3 1.0
CD A:LYS345 4.3 11.3 1.0
CG A:LYS348 4.3 10.4 1.0
OD2 A:ASP352 4.4 6.0 1.0
CG A:LEU349 4.5 8.3 1.0

Reference:

S.M.Wilbanks, D.B.Mckay. How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site. J.Biol.Chem. V. 270 2251 1995.
ISSN: ISSN 0021-9258
PubMed: 7836458
DOI: 10.1074/JBC.270.5.2251
Page generated: Sat Dec 12 08:37:14 2020

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