Structure of PDB 1l2c Chain A Binding Site BS02

Receptor Information

>1l2c Chain A (length=259) Species: 1422 (Geobacillus stearothermophilus)

PELPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKFGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDQTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMKGGSFQHHLYVYGRQGNPCKRCGTPIEKTVVAGRG
THYCPRCQR

Ligand information

>1l2c Chain C (length=12)

gtccacgtctac

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1l2c Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM.
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): E3 K60 H74 R76 M77 R112 F114 Q166 N174 I175 Y242 K258 R264
• Binding residue (residue number reindexed from 1): E2 K59 H73 R75 M76 R111 F113 Q165 N173 I174 Y227 K243 R249

Enzymatic activity

• Enzyme Commision number: 3.2.2.23: DNA-formamidopyrimidine glycosylase.
  4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.

Gene Ontology

Molecular Function

• GO:0003676 nucleic acid binding
• GO:0003677 DNA binding
• GO:0003684 damaged DNA binding
• GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
• GO:0008270 zinc ion binding
• GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
• GO:0016787 hydrolase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
• GO:0016829 lyase activity
• GO:0019104 DNA N-glycosylase activity
• GO:0034039 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
• GO:0046872 metal ion binding
• GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease activity

Biological Process

• GO:0006281 DNA repair
• GO:0006284 base-excision repair

External links

• PDB: RCSB:1l2c, PDBe:1l2c, PDBj:1l2c
• PDBsum: 1l2c
• PubMed: 12055620
• UniProt: P84131