Structure of PDB 5kn9 Chain A

Receptor sequence
>5kn9A (length=222) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
FPAREFQRDLLDWFARERRDLPWRKDRDPYKVWVSEVMLQQTRYETVIPY
FEQFIDRFPTLEALADADEDEVLKAWEGLGYYSRVRNLHAAVKEVKTRYG
GKVPDDPDEFSRLKGVGPYTVGAVLSLAYGVPEPAVNGNVMRVLSRLFLV
TDDIAKCSTRKRFEQIVREIMAYENPGAFNEALIELGALVCTPRRPSCLL
CPVQAYCQAFAEGVAEELPVKM
3D structure
PDB5kn9 Structural Basis for the Lesion-scanning Mechanism of the MutY DNA Glycosylase.
ChainA
Resolution1.93 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) E43 Y126 N144
Catalytic site (residue number reindexed from 1) E36 Y119 N137
Enzyme Commision number 3.2.2.31: adenine 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 G87 Y88 K163 C164 S165 G80 Y81 K156 C157 S158
BS02 dna A Q47 G122 G124 P125 Y126 T127 N144 G145 R167 K228 Q40 G115 G117 P118 Y119 T120 N137 G138 R160 K221
BS03 SF4 A R153 C198 C205 C208 C214 R146 C191 C198 C201 C207
BS04 CA A S118 V123 S111 V116
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003824 catalytic activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0019104 DNA N-glycosylase activity
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5kn9, PDBe:5kn9, PDBj:5kn9
PDBsum5kn9
PubMed28130451
UniProtP83847|MUTY_GEOSE Adenine DNA glycosylase (Gene Name=mutY)

[Back to BioLiP]