Structure of PDB 1diz Chain A Binding Site BS02

Receptor Information
>1diz Chain A (length=282) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MYTLNWQPPYDWSWMLGFLAARAVSSVETVADSYYARSLAVGEYRGVVTA
IPDIARHTLHINLSAGLEPVAAECLAKMSRLFDLQCNPQIVNGALGRLGA
ARPGLRLPGCVDAFEQGVRAILGQLVSVAMAAKLTARVAQLYGERLDDFP
EYICFPTPQRLAAADPQALKALGMPLKRAEALIHLANAALEGTLPMTIPG
DVEQAMKTLQTFPGIGRWTANYFALRGWQAKDVFLPDDYLIKQRFPGMTP
AQIRRYAERWKPWRSYALLHIWYTEGWQPDEA
Ligand information
Receptor-Ligand Complex Structure
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PDB1diz DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA.
Resolution2.5 Å
Binding residue
(original residue number in PDB)
L125 M130 M174 P175
Binding residue
(residue number reindexed from 1)
L125 M130 M174 P175
Enzymatic activity
Catalytic site (original residue number in PDB) W218 Y222 D238
Catalytic site (residue number reindexed from 1) W218 Y222 D238
Enzyme Commision number 3.2.2.21: DNA-3-methyladenine glycosylase II.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003905 alkylbase DNA N-glycosylase activity
GO:0005515 protein binding
GO:0008725 DNA-3-methyladenine glycosylase activity
GO:0016787 hydrolase activity
GO:0032131 alkylated DNA binding
GO:0043916 DNA-7-methylguanine glycosylase activity
GO:0052821 DNA-7-methyladenine glycosylase activity
GO:0052822 DNA-3-methylguanine glycosylase activity
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006285 base-excision repair, AP site formation
GO:0006307 DNA alkylation repair
GO:0006950 response to stress
GO:0006974 DNA damage response
Cellular Component
GO:0005737 cytoplasm
GO:0032993 protein-DNA complex

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Cellular Component
External links
PDB RCSB:1diz, PDBe:1diz, PDBj:1diz
PDBsum1diz
PubMed10675345
UniProtP04395|3MG2_ECOLI DNA-3-methyladenine glycosylase 2 (Gene Name=alkA)

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