Structure of PDB 4uqm Chain A

Receptor sequence
>4uqmA (length=229) Species: 1299 (Deinococcus radiodurans) [Search protein sequence]
RPIIPANLPEDWQEALLPEFSAPYFHELTDFLRQERKEYTIYPPAPDVFN
ALRYTPLGEVKVLILGQDPYHGPNQAHGLSFSVRPGVRVPPSLRNIYKEL
TEDIPGFVAPKHGYLRSWAEQGVLLLNAVLTVRAAQANSHQGKGWEHFTD
AVIKAVNAKEERVVFILWGSYARKKKKLITGKNHVVIESGHPSPLSEQYF
FGTRPFSKTNEALEKAGRGPVEWQLPATV
3D structure
PDB4uqm Structure determination of uracil-DNA N-glycosylase from Deinococcus radiodurans in complex with DNA.
ChainA
Resolution1.35 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) D83 Y85 F96 H206
Catalytic site (residue number reindexed from 1) D68 Y70 F81 H191
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 A D83 H86 P106 S107 G184 S185 G205 H206 S208 P209 L210 S211 Y214 D68 H71 P91 S92 G169 S170 G190 H191 S193 P194 L195 S196 Y199
BS02 dna A R103 L210 E212 R88 L195 E197
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:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4uqm, PDBe:4uqm, PDBj:4uqm
PDBsum4uqm
PubMed26457437
UniProtQ9RWH9|UNG_DEIRA Uracil-DNA glycosylase (Gene Name=ung)

[Back to BioLiP]