Structure of PDB 5nnu Chain E

Receptor sequence
>5nnuE (length=222) Species: 37296 (Human gammaherpesvirus 8) [Search protein sequence]
DLLLAPKWISFLSLSSFLKQKLLSLLRQIRELRLTTTVYPPQDKLMWWSH
CCDPEDIKVVILGQDPYHKGQATGLAFSVDPQCQVPPSLRSIFRELEASV
PNFSTPSHGCLDSWARQGVLLLNTVLTVEKGGWDWFTSFIISSISSKLEH
CVFLLWGRKAIDRTPLINAQKHLVLTAQHPSPLASLGGRHSRWPRFQGCN
HFNLANDYLTRHRRETVDWGLL
3D structure
PDB5nnu A structurally conserved motif in gamma-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping.
ChainE
Resolution2.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D91 Y93 F103 H213
Catalytic site (residue number reindexed from 1) D65 Y67 F77 H179
Enzyme Commision number 3.2.2.27: uracil-DNA glycosylase.
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 dna E S39 F173 S180 K181 S13 F139 S146 K147
BS02 dna E D91 P113 S114 G191 R192 Q212 H213 S215 P216 L217 A218 G221 G222 S225 D65 P87 S88 G157 R158 Q178 H179 S181 P182 L183 A184 G187 G188 S191
BS03 dna E R116 S219 L220 R223 R90 S185 L186 R189
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

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Molecular Function

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Cellular Component
External links
PDB RCSB:5nnu, PDBe:5nnu, PDBj:5nnu
PDBsum5nnu
PubMed29596604
UniProtF5HFA1|UNG_HHV8P Uracil-DNA glycosylase (Gene Name=ORF46)

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