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Zinc in PDB 2k1q: uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor

Other elements in 2k1q:

The structure of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor also contains other interesting chemical elements:

Fluorine (F) 40 atoms
Chlorine (Cl) 20 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor (pdb code 2k1q). 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 uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor, PDB code: 2k1q:

Zinc binding site 1 out of 1 in 2k1q

Go back to Zinc Binding Sites List in 2k1q
Zinc binding site 1 out of 1 in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:0.0
occ:1.00
SG A:CYS97 2.3 0.0 1.0
SG A:CYS99 2.3 0.0 1.0
SG A:CYS145 2.3 0.0 1.0
H A:THR98 2.5 0.0 1.0
HA A:CYS97 2.7 0.0 1.0
HB2 A:HIS149 3.0 0.0 1.0
N A:THR98 3.1 0.0 1.0
HB2 A:SER147 3.1 0.0 1.0
H A:CYS99 3.2 0.0 1.0
HB3 A:CYS99 3.2 0.0 1.0
HD1 A:HIS149 3.2 0.0 1.0
CA A:CYS97 3.3 0.0 1.0
CB A:CYS145 3.3 0.0 1.0
CB A:CYS97 3.3 0.0 1.0
CB A:CYS99 3.4 0.0 1.0
HB2 A:CYS145 3.4 0.0 1.0
HB3 A:CYS145 3.5 0.0 1.0
N A:CYS99 3.5 0.0 1.0
C A:CYS97 3.5 0.0 1.0
HG A:SER147 3.8 0.0 1.0
HB2 A:CYS97 3.8 0.0 1.0
CB A:SER147 4.0 0.0 1.0
C A:THR98 4.0 0.0 1.0
ND1 A:HIS149 4.0 0.0 1.0
OG A:SER147 4.0 0.0 1.0
CB A:HIS149 4.1 0.0 1.0
CA A:CYS99 4.1 0.0 1.0
HG22 A:THR98 4.1 0.0 1.0
CA A:THR98 4.2 0.0 1.0
HB2 A:SER101 4.2 0.0 1.0
HB2 A:CYS99 4.2 0.0 1.0
HB3 A:CYS97 4.2 0.0 1.0
HG11 A:VAL151 4.3 0.0 1.0
HB3 A:SER147 4.4 0.0 1.0
H A:HIS149 4.4 0.0 1.0
H A:SER101 4.5 0.0 1.0
H A:GLY100 4.5 0.0 1.0
H A:SER147 4.5 0.0 1.0
HB3 A:HIS149 4.5 0.0 1.0
CG A:HIS149 4.5 0.0 1.0
O A:CYS97 4.6 0.0 1.0
H A:CYS145 4.6 0.0 1.0
HG13 A:VAL151 4.7 0.0 1.0
N A:CYS97 4.7 0.0 1.0
CA A:CYS145 4.8 0.0 1.0
H A:GLY148 4.8 0.0 1.0
O A:THR98 4.8 0.0 1.0
HA A:THR98 4.8 0.0 1.0
C A:CYS99 4.9 0.0 1.0
O A:HIS149 4.9 0.0 1.0
CG2 A:THR98 4.9 0.0 1.0
CG1 A:VAL151 5.0 0.0 1.0
N A:GLY100 5.0 0.0 1.0
HA A:CYS99 5.0 0.0 1.0
N A:HIS149 5.0 0.0 1.0
HG23 A:THR98 5.0 0.0 1.0

Reference:

M.Gallo, M.Pennestri, M.J.Bottomley, G.Barbato, T.Eliseo, M.Paci, F.Narjes, R.De Francesco, V.Summa, U.Koch, R.Bazzo, D.O.Cicero. Binding of A Noncovalent Inhibitor Exploiting the S' Region Stabilizes the Hepatitis C Virus NS3 Protease Conformation in the Absence of Cofactor. J.Mol.Biol. V. 385 1142 2009.
ISSN: ISSN 0022-2836
PubMed: 19061898
DOI: 10.1016/J.JMB.2008.11.017
Page generated: Wed Dec 16 03:33:27 2020

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