Structure of PDB 1mud Chain A

Receptor sequence
>1mudA (length=225) Species: 562 (Escherichia coli) [Search protein sequence]
MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIP
YFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLH
GGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILNGNVKRVLARCYA
VSGWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCS
LCPLQNGCIAAANNSWALYPGKKPK
3D structure
PDB1mud MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily.
ChainA
Resolution1.8 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 N138
Catalytic site (residue number reindexed from 1) E37 S120 N138
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 C199 C202 Q205 C208 R147 C192 C199 C202 Q205 C208
BS02 ADE A E37 L40 Q182 M185 E37 L40 Q182 M185
BS03 ADE A T193 S195 T193 S195
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:1mud, PDBe:1mud, PDBj:1mud
PDBsum1mud
PubMed9846876
UniProtP17802|MUTY_ECOLI Adenine DNA glycosylase (Gene Name=mutY)

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