Structure of PDB 5nnu Chain D Binding Site BS02

Receptor Information
>5nnu Chain D (length=230) Species: 37296 (Human gammaherpesvirus 8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLLLAPKWISFLSLSSFLKQKLLSLLRQIRELRLTTTVYPPQDKLMWWSH
CCDPEDIKVVILGQDPYHKGQATGLAFSVDPQCQVPPSLRSIFRELEASV
PNFSTPSHGCLDSWARQGVLLLNTVLTVEKGRAGSHEGLGWDWFTSFIIS
SISSKLEHCVFLLWGRKAIDRTPLINAQKHLVLTAQHPSPLASLGGRHSR
WPRFQGCNHFNLANDYLTRHRRETVDWGLL
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5nnu A structurally conserved motif in gamma-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping.
Resolution2.97 Å
Binding residue
(original residue number in PDB)		Q90 D91 P113 S114 G191 R192 Q212 H213 S215 P216 L217 A218 G221 G222 S225
Binding residue
(residue number reindexed from 1)		Q64 D65 P87 S88 G165 R166 Q186 H187 S189 P190 L191 A192 G195 G196 S199
Enzymatic activity
Catalytic site (original residue number in PDB) D91 Y93 F103 H213
Catalytic site (residue number reindexed from 1) D65 Y67 F77 H187
Enzyme Commision number 3.2.2.27: uracil-DNA glycosylase.
Gene Ontology
Molecular Function
GO:0004844 uracil DNA N-glycosylase activity
GO:0016787 hydrolase activity
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0097510 base-excision repair, AP site formation via deaminated base removal
Cellular Component
GO:0042025 host cell nucleus

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5nnu, PDBe:5nnu, PDBj:5nnu
PDBsum5nnu
PubMed29596604
UniProtF5HFA1|UNG_HHV8P Uracil-DNA glycosylase (Gene Name=ORF46)

[Back to BioLiP]