Structure of PDB 4cis Chain A Binding Site BS03

Receptor Information
>4cis Chain A (length=263) Species: 1359 (Lactococcus cremoris) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PELPEVETVRRELEKRIVGQKIISIEATYPRMVLTGFEQLKKELTGKIIQ
GIIRRGKYLIFEIGDDFRLISHLRMEGKYRLATLDAPREKHDHLTMKFSD
GQLIYADVRKFGTWELISTDQVLPYFLNKKIGPEPTYEDFDEKLFREKLR
KSTKKIKPYLLEQTLVAGLGNIYVDEVLWLAKIHPEKEANQLIESSIHLL
HDSIIEILQKAIKLGGSSITGKMQNELQVYGKTGEKCSRCGAEIQKIKVA
GRGTHFCPFCQQK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4cis Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4cis Ribose-protonated DNA base excision repair: a combined theoretical and experimental study.
Resolution2.05 Å
Binding residue
(original residue number in PDB)
C245 C248 C265 C268
Binding residue
(residue number reindexed from 1)
C237 C240 C257 C260
Annotation score1
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4cis, PDBe:4cis, PDBj:4cis
PDBsum4cis
PubMed25065673
UniProtQ031W6

[Back to BioLiP]