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Calcium in PDB 3st9: Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus

Enzymatic activity of Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus

All present enzymatic activity of Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus:
3.4.21.92;

Protein crystallography data

The structure of Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus, PDB code: 3st9 was solved by J.Zhang, F.Ye, L.Lan, H.Jiang, C.Luo, C.-G.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.43
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 121.289, 121.289, 404.377, 90.00, 90.00, 120.00
R / Rfree (%) 23.9 / 27.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus (pdb code 3st9). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus, PDB code: 3st9:

Calcium binding site 1 out of 1 in 3st9

Go back to Calcium Binding Sites List in 3st9
Calcium binding site 1 out of 1 in the Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Clpp in Heptameric Form From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca196

b:85.3
occ:1.00
N B:ASP59 3.5 49.3 1.0
CA B:LYS58 3.8 50.7 1.0
CB B:LYS58 4.1 50.7 1.0
CB B:ASP59 4.2 48.5 1.0
C B:LYS58 4.2 50.0 1.0
CG B:ASP59 4.3 49.2 1.0
CG B:LYS58 4.3 51.8 1.0
OD2 B:ASP59 4.4 49.8 1.0
CA B:ASP59 4.4 48.4 1.0
OD1 B:ASP59 4.8 50.7 1.0
OH B:TYR61 4.9 46.0 1.0

Reference:

J.Zhang, F.Ye, L.Lan, H.Jiang, C.Luo, C.-G.Yang. Structural Switching of Staphylococcus Aureus Clp Protease: A Key to Understanding Protease Dynamics J.Biol.Chem. V. 286 37590 2011.
ISSN: ISSN 0021-9258
PubMed: 21900233
DOI: 10.1074/JBC.M111.277848
Page generated: Sat Dec 12 04:30:33 2020

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