Structure of PDB 5nnu Chain D

Receptor sequence
>5nnuD (length=230) Species: 37296 (Human gammaherpesvirus 8) [Search protein sequence]
DLLLAPKWISFLSLSSFLKQKLLSLLRQIRELRLTTTVYPPQDKLMWWSH
CCDPEDIKVVILGQDPYHKGQATGLAFSVDPQCQVPPSLRSIFRELEASV
PNFSTPSHGCLDSWARQGVLLLNTVLTVEKGRAGSHEGLGWDWFTSFIIS
SISSKLEHCVFLLWGRKAIDRTPLINAQKHLVLTAQHPSPLASLGGRHSR
WPRFQGCNHFNLANDYLTRHRRETVDWGLL
3D structure
PDB5nnu A structurally conserved motif in gamma-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping.
ChainD
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 H187
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 D S39 F173 S180 K181 S13 F147 S154 K155
BS02 dna D Q90 D91 P113 S114 G191 R192 Q212 H213 S215 P216 L217 A218 G221 G222 S225 Q64 D65 P87 S88 G165 R166 Q186 H187 S189 P190 L191 A192 G195 G196 S199
BS03 dna D R120 P216 S219 L220 R223 R94 P190 S193 L194 R197
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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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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