Structure of PDB 2eug Chain A

Receptor sequence
>2eugA (length=225) Species: 37762 (Escherichia coli B) [Search protein sequence]
LTWHDVLAEEKQQPHFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELG
DVKVVILGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFT
RPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQ
HREGVVFLLWGSHAQKKGAIIDKQRHHVLKAPHPSPLSAHRGFFGCNHFV
LANQWLEQHGETPIDWMPVLPAESE
3D structure
PDB2eug Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) D64 Y66 F77 H187
Catalytic site (residue number reindexed from 1) D60 Y62 F73 H183
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 URA A G62 Q63 D64 Y66 A76 F77 N123 G58 Q59 D60 Y62 A72 F73 N119
Gene Ontology
Molecular Function
GO:0004844 uracil DNA N-glycosylase activity
GO:0005515 protein binding
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:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2eug, PDBe:2eug, PDBj:2eug
PDBsum2eug
PubMed10090282
UniProtP12295|UNG_ECOLI Uracil-DNA glycosylase (Gene Name=ung)

[Back to BioLiP]