Structure of PDB 1muy Chain A

Receptor sequence
>1muyA (length=225) Species: 562 (Escherichia coli) [Search protein sequence]
MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIP
YFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLH
GGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYA
VSGWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCS
LCPLQNGCIAAANNSWALYPGKKPK
3D structure
PDB1muy MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E37 S120 D138
Catalytic site (residue number reindexed from 1) E37 S120 D138
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 SF4 A R147 C192 P197 C199 C202 Q205 C208 R147 C192 P197 C199 C202 Q205 C208
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1muy, PDBe:1muy, PDBj:1muy
PDBsum1muy
PubMed9846876
UniProtP17802|MUTY_ECOLI Adenine DNA glycosylase (Gene Name=mutY)

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