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Zinc in PDB 5u4p: Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31

Enzymatic activity of Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31

All present enzymatic activity of Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31:
3.4.19.12;

Protein crystallography data

The structure of Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31, PDB code: 5u4p was solved by E.J.Worden, K.C.Dong, A.Martin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 109.30 / 2.50
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 126.210, 126.210, 139.870, 90.00, 90.00, 120.00
R / Rfree (%) 21.1 / 23.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31 (pdb code 5u4p). 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 Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31, PDB code: 5u4p:

Zinc binding site 1 out of 1 in 5u4p

Go back to Zinc Binding Sites List in 5u4p
Zinc binding site 1 out of 1 in the Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Protein-Protein Complex Between 26S Proteasome Regulatory Subunit RPN8, RPN11, and Ubiquitin S31 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:98.3
occ:1.00
 OD2 B:ASP122 1.9 78.2 1.0
NE2 B:HIS111 1.9 83.4 1.0
O C:GLY76 2.0 71.9 1.0
NE2 B:HIS109 2.3 65.9 1.0
CE1 B:HIS111 2.7 77.8 1.0
HE1 B:HIS111 2.8 0.9 1.0
CG B:ASP122 3.0 76.7 1.0
CD2 B:HIS111 3.1 75.2 1.0
C C:GLY76 3.2 70.5 1.0
CE1 B:HIS109 3.2 64.1 1.0
CD2 B:HIS109 3.3 63.5 1.0
HE1 B:HIS109 3.4 0.5 1.0
HD2 B:HIS111 3.4 0.2 1.0
H B:SER119 3.4 0.7 1.0
HD2 B:HIS109 3.4 0.1 1.0
OD1 B:ASP122 3.4 83.5 1.0
HB3 B:SER119 3.5 96.9 1.0
H C:GLY76 3.6 0.7 1.0
OXT C:GLY76 3.7 79.0 1.0
ND1 B:HIS111 3.9 82.2 1.0
O B:TRP117 4.0 68.2 1.0
HG B:SER119 4.0 95.4 1.0
CG B:HIS111 4.1 77.0 1.0
OG B:SER119 4.1 74.1 1.0
HA B:LEU118 4.1 0.5 1.0
N C:GLY76 4.1 76.0 1.0
HG11 B:VAL140 4.2 83.7 1.0
CB B:SER119 4.2 74.7 1.0
N B:SER119 4.2 73.2 1.0
CA C:GLY76 4.2 80.4 1.0
CB B:ASP122 4.2 76.4 1.0
HG13 B:VAL140 4.3 83.7 1.0
HB2 B:ASP122 4.3 0.4 1.0
ND1 B:HIS109 4.3 64.8 1.0
CG B:HIS109 4.4 62.2 1.0
HB3 B:ASP122 4.5 0.4 1.0
HG21 B:VAL140 4.5 95.3 1.0
HG22 B:VAL140 4.6 95.3 1.0
HD1 B:HIS111 4.6 0.3 1.0
CG1 B:VAL140 4.7 63.2 1.0
HA3 C:GLY76 4.8 0.5 1.0
CA B:SER119 4.9 75.4 1.0
HE2 B:PHE114 4.9 88.9 1.0
HA2 C:GLY76 4.9 0.5 1.0
CA B:LEU118 4.9 72.8 1.0
HD23 B:LEU118 4.9 93.1 1.0
HB2 B:SER119 5.0 96.9 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 09:07:17 2024

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