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BioLiP

Structure of PDB 1emh Chain A

Receptor sequence
>1emhA (length=223) Species: 9606 (Homo sapiens) [Search protein sequence]
MEFFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQM
CDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDI
EDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVS
WLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGC
RHFSKTNELLQKSGKKPIDWKEL
3D structure
PDB1emh Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
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 Q144 D145 Y147 H148 C157 F158 P168 S169 N204 G246 S247 H268 S270 P271 L272 S273 R276 Q63 D64 Y66 H67 C76 F77 P87 S88 N123 G165 S166 H187 S189 P190 L191 S192 R195
Gene Ontology
Molecular Function
GO:0004844 uracil DNA N-glycosylase activity
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:1emh, PDBe:1emh, PDBj:1emh
PDBsum1emh
PubMed10805771
UniProtP13051|UNG_HUMAN Uracil-DNA glycosylase (Gene Name=UNG)

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