Structure of PDB 2brk Chain A

Receptor sequence
>2brkA (length=512) [Search protein sequence]
SMSYTWTGALITPCAAEESKLMVYATTSRSAGLRQKKVTFDRLQVLDDHY
RDVLKEMKAKASTVKAKLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSK
AVNHIHSVWKDLLEDTVTPIDTTIMAKNEVFCVGRKPARLIVFPDLGVRV
CEKMALYDVVSTLPQVVMGSSYGFQYSPGQRVEFLVNTWKSKKNPMGFSY
DTRCFDSTVTENDIRVEESIYQCCDLAPEARQAIKSLTERLYIGGPLTNS
KGQNCGYRRCRASGVLTTSCGNTLTCYLKASAACRAAKLQDCTMLVNGDD
LVVICESAGTQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITSCSSN
VSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTL
WARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIERLHGL
SAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAA
TCGKYLFNWAVK
3D structure
PDB2brk Interdomain Communication in Hepatitis C Virus Polymerase Abolished by Small-Molecule Inhibitors Bound to a Novel Allosteric Site
ChainA
Resolution2.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.7.7.48: RNA-directed RNA polymerase.
3.4.21.98: hepacivirin.
3.4.22.-
3.6.1.15: nucleoside-triphosphate phosphatase.
3.6.4.13: RNA helicase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 MN A D220 T221 D318 D201 T202 D299
BS02 MN A D220 D318 D319 D201 D299 D300
BS03 CMF A V37 L392 A393 A396 H428 L492 G493 P495 R503 V23 L373 A374 A377 H409 L473 G474 P476 R484
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003968 RNA-dependent RNA polymerase activity
Biological Process
GO:0039694 viral RNA genome replication

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2brk, PDBe:2brk, PDBj:2brk
PDBsum2brk
PubMed15955819
UniProtP26663|POLG_HCVBK Genome polyprotein

[Back to BioLiP]