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Chlorine 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
Zinc (Zn) 20 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine 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:

Chlorine binding site 1 out of 1 in 2k1q

Go back to Chlorine Binding Sites List in 2k1q
Chlorine 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 Chlorine with other atoms in the Cl 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
B:Cl191

b:0.0
occ:1.00
CLD1 B:FE3191 0.0 0.0 1.0
CD1 B:FE3191 1.5 0.0 1.0
H2B B:FE3191 2.5 0.0 1.0
CG B:FE3191 2.5 0.0 1.0
CE1 B:FE3191 2.5 0.0 1.0
HN B:FE3191 2.7 0.0 1.0
HE1 B:FE3191 2.7 0.0 1.0
N B:FE3191 2.9 0.0 1.0
CB B:FE3191 2.9 0.0 1.0
HA B:OBF190 3.0 0.0 1.0
OE1 A:GLN41 3.1 0.0 1.0
C B:OBF190 3.2 0.0 1.0
CA B:OBF190 3.5 0.0 1.0
CA B:FE3191 3.5 0.0 1.0
O B:LEU189 3.6 0.0 1.0
HE3 A:LYS136 3.7 0.0 1.0
CD2 B:FE3191 3.8 0.0 1.0
CZ B:FE3191 3.8 0.0 1.0
H1B B:FE3191 3.9 0.0 1.0
N B:OBF190 3.9 0.0 1.0
O B:OBF190 3.9 0.0 1.0
C B:LEU189 4.0 0.0 1.0
HD2 A:HIS57 4.0 0.0 1.0
CD A:GLN41 4.0 0.0 1.0
HB3 B:LEU189 4.1 0.0 1.0
H2A B:FE3191 4.2 0.0 1.0
HD2 A:LYS136 4.2 0.0 1.0
H1A B:FE3191 4.3 0.0 1.0
CE2 B:FE3191 4.4 0.0 1.0
HE22 A:GLN41 4.6 0.0 1.0
HN B:OBF190 4.6 0.0 1.0
CD2 A:HIS57 4.6 0.0 1.0
HB2 A:GLN41 4.6 0.0 1.0
CE A:LYS136 4.6 0.0 1.0
NE2 A:GLN41 4.7 0.0 1.0
HD2 B:FE3191 4.7 0.0 1.0
HG3 A:GLN41 4.8 0.0 1.0
CD A:LYS136 4.8 0.0 1.0
HB3 A:GLN41 4.8 0.0 1.0
NE2 A:HIS57 4.8 0.0 1.0
CG A:GLN41 4.9 0.0 1.0
CB B:LEU189 4.9 0.0 1.0
HB2 B:LEU189 4.9 0.0 1.0
HA2 A:GLY58 4.9 0.0 1.0
CB B:OBF190 4.9 0.0 1.0
HD3 A:LYS136 5.0 0.0 1.0
CF B:FE3191 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: Sat Dec 12 09:11:27 2020

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