Zinc in PDB 5vfr: Nucleotide-Driven Triple-State Remodeling of the Aaa-Atpase Channel in the Activated Human 26S Proteasome

Enzymatic activity of Nucleotide-Driven Triple-State Remodeling of the Aaa-Atpase Channel in the Activated Human 26S Proteasome

All present enzymatic activity of Nucleotide-Driven Triple-State Remodeling of the Aaa-Atpase Channel in the Activated Human 26S Proteasome:
3.4.25.1;

Zinc Binding Sites:

The binding sites of Zinc atom in the Nucleotide-Driven Triple-State Remodeling of the Aaa-Atpase Channel in the Activated Human 26S Proteasome (pdb code 5vfr). 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 Nucleotide-Driven Triple-State Remodeling of the Aaa-Atpase Channel in the Activated Human 26S Proteasome, PDB code: 5vfr:

Zinc binding site 1 out of 1 in 5vfr

Go back to Zinc Binding Sites List in 5vfr
Zinc binding site 1 out of 1 in the Nucleotide-Driven Triple-State Remodeling of the Aaa-Atpase Channel in the Activated Human 26S Proteasome


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Nucleotide-Driven Triple-State Remodeling of the Aaa-Atpase Channel in the Activated Human 26S Proteasome within 5.0Å range:
probe atom residue distance (Å) B Occ
c:Zn401

b:0.1
occ:1.00
N c:SER114 2.2 0.2 1.0
O c:SER114 2.2 0.2 1.0
C c:SER114 2.6 0.2 1.0
CD2 c:HIS113 2.7 0.0 1.0
CB c:HIS113 2.8 0.0 1.0
CA c:SER114 2.9 0.2 1.0
CD2 c:HIS115 3.0 0.6 1.0
O c:VAL53 3.0 0.8 1.0
CG c:HIS113 3.0 0.0 1.0
C c:HIS113 3.0 0.0 1.0
CA c:HIS113 3.4 0.0 1.0
NE2 c:HIS115 3.4 0.6 1.0
N c:HIS115 3.6 0.6 1.0
CG c:HIS115 4.0 0.6 1.0
O c:HIS113 4.0 0.0 1.0
N c:VAL53 4.0 0.8 1.0
NE2 c:HIS113 4.0 0.0 1.0
CB c:SER114 4.0 0.2 1.0
C c:VAL53 4.1 0.8 1.0
CB c:GLU52 4.1 0.0 1.0
CA c:HIS115 4.3 0.6 1.0
ND1 c:HIS113 4.4 0.0 1.0
CE1 c:HIS115 4.5 0.6 1.0
CA c:GLU52 4.7 0.0 1.0
CB c:HIS115 4.7 0.6 1.0
C c:GLU52 4.7 0.0 1.0
ND1 c:HIS115 4.7 0.6 1.0
CA c:VAL53 4.7 0.8 1.0
N c:HIS113 4.7 0.0 1.0
CE1 c:HIS113 4.8 0.0 1.0
OG c:SER114 4.9 0.2 1.0
OD2 c:ASP126 5.0 0.4 1.0

Reference:

Y.Zhu, W.L.Wang, D.Yu, Q.Ouyang, Y.Lu, Y.Mao. Structural Mechanism For Nucleotide-Driven Remodeling of the Aaa-Atpase Unfoldase in the Activated Human 26S Proteasome. Nat Commun V. 9 1360 2018.
ISSN: ESSN 2041-1723
PubMed: 29636472
DOI: 10.1038/S41467-018-03785-W
Page generated: Wed Dec 16 11:09:56 2020

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