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Zinc in PDB 5w83: RPN8/RPN11 Dimer Complex

Enzymatic activity of RPN8/RPN11 Dimer Complex

All present enzymatic activity of RPN8/RPN11 Dimer Complex:
3.4.19.12;

Protein crystallography data

The structure of RPN8/RPN11 Dimer Complex, PDB code: 5w83 was solved by K.C.Dong, E.J.Worden, A.Martin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.48 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.720, 74.990, 82.470, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 23.4

Zinc Binding Sites:

The binding sites of Zinc atom in the RPN8/RPN11 Dimer Complex (pdb code 5w83). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the RPN8/RPN11 Dimer Complex, PDB code: 5w83:

Zinc binding site 1 out of 1 in 5w83

Go back to Zinc Binding Sites List in 5w83
Zinc binding site 1 out of 1 in the RPN8/RPN11 Dimer Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of RPN8/RPN11 Dimer Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:30.6
occ:0.00
NE2 B:HIS109 2.1 22.0 1.0
O B:HOH473 2.3 34.5 1.0
OD1 B:ASP122 2.4 28.1 1.0
OE2 B:GLU48 2.5 43.7 1.0
OD2 B:ASP122 2.5 27.2 1.0
NE2 B:HIS111 2.6 30.0 1.0
CD2 B:HIS109 2.8 25.2 1.0
CG B:ASP122 2.8 26.9 1.0
HD2 B:HIS109 2.8 30.2 1.0
HD2 B:HIS111 3.1 34.0 1.0
CE1 B:HIS109 3.2 26.2 1.0
CD2 B:HIS111 3.2 28.3 1.0
CD B:GLU48 3.5 45.1 1.0
HE1 B:HIS109 3.6 31.4 1.0
O B:HOH434 3.7 56.0 1.0
CE1 B:HIS111 3.7 33.6 1.0
O B:HOH451 3.9 48.9 1.0
OE1 B:GLU48 3.9 53.8 1.0
HG B:SER119 3.9 38.4 1.0
CG B:HIS109 4.0 20.8 1.0
HE1 B:HIS111 4.0 40.3 1.0
H B:SER119 4.1 31.0 1.0
OG B:SER119 4.1 32.0 1.0
ND1 B:HIS109 4.2 26.2 1.0
CB B:ASP122 4.3 27.9 1.0
HB3 B:SER119 4.4 39.2 1.0
CG B:HIS111 4.5 27.6 1.0
HB3 B:GLU48 4.6 41.7 1.0
HB3 B:ASP122 4.6 33.4 1.0
HB2 B:ASP122 4.7 33.4 1.0
ND1 B:HIS111 4.7 26.3 1.0
HE2 B:PHE114 4.7 34.2 1.0
CG B:GLU48 4.8 35.4 1.0
CB B:SER119 4.8 32.7 1.0
HA B:LEU118 4.9 35.0 1.0
HG2 B:GLU48 4.9 42.5 1.0
O B:SER110 4.9 27.1 1.0
HD1 B:HIS109 5.0 31.4 1.0
H B:ASP122 5.0 38.5 1.0
N B:SER119 5.0 25.8 1.0
O B:HOH504 5.0 53.5 1.0

Reference:

E.J.Worden, K.C.Dong, A.Martin. An Aaa Motor-Driven Mechanical Switch in RPN11 Controls Deubiquitination at the 26S Proteasome. Mol. Cell V. 67 799 2017.
ISSN: ISSN 1097-4164
PubMed: 28844860
DOI: 10.1016/J.MOLCEL.2017.07.023
Page generated: Mon Oct 28 13:54:20 2024

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