Structure of PDB 4g4q Chain A Binding Site BS02

Receptor Information

>4g4q Chain A (length=254) Species: 1422 (Geobacillus stearothermophilus)

PELPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKAGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDCTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMKHHLYVYGRQGNPCKRCGTPIEKTVVAGRGTHYCP
RCQR

Ligand information

>4g4q Chain C (length=11)

gtccgagtcta

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4g4q Structural and Biochemical Analysis of DNA Helix Invasion by the Bacterial 8-Oxoguanine DNA Glycosylase MutM.
• Resolution: 1.86 Å
• Binding residue (original residue number in PDB): H74 R76 P130 L134 C166 T167 R264 G265
• Binding residue (residue number reindexed from 1): H73 R75 P129 L133 C165 T166 R244 G245

Enzymatic activity

• Catalytic site (original residue number in PDB): P2 E3
• Catalytic site (residue number reindexed from 1): P1 E2
• 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:4g4q, PDBe:4g4q, PDBj:4g4q
• PDBsum: 4g4q
• PubMed: 23404556
• UniProt: P84131