Structure of PDB 4cis Chain A Binding Site BS02

Receptor Information

>4cis Chain A (length=263) Species: 1359 (Lactococcus cremoris)

PELPEVETVRRELEKRIVGQKIISIEATYPRMVLTGFEQLKKELTGKIIQ
GIIRRGKYLIFEIGDDFRLISHLRMEGKYRLATLDAPREKHDHLTMKFSD
GQLIYADVRKFGTWELISTDQVLPYFLNKKIGPEPTYEDFDEKLFREKLR
KSTKKIKPYLLEQTLVAGLGNIYVDEVLWLAKIHPEKEANQLIESSIHLL
HDSIIEILQKAIKLGGSSITGKMQNELQVYGKTGEKCSRCGAEIQKIKVA
GRGTHFCPFCQQK

Ligand information

>4cis Chain D (length=14)

ctctttgtttctcg

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4cis Ribose-protonated DNA base excision repair: a combined theoretical and experimental study.
• Resolution: 2.05 Å
• Binding residue (original residue number in PDB): K57 H72 R74 M75 K129 L161 E162 Q163 G170 R260
• Binding residue (residue number reindexed from 1): K57 H72 R74 M75 K129 L161 E162 Q163 G170 R252

Enzymatic activity

• Catalytic site (original residue number in PDB): P1 E2
• 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:4cis, PDBe:4cis, PDBj:4cis
• PDBsum: 4cis
• PubMed: 25065673
• UniProt: Q031W6