Structure of PDB 2kqd Chain A Binding Site BS03
Receptor Information
>2kqd Chain A (length=55) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
GPLGSGSEGNKVKRTSCMYGANCYRKNPVHFQHFSHPGDSDYGGVQIVGQ
DETDD
Ligand information
Ligand ID
RIB
InChI
InChI=1S/C5H10O5/c6-1-2-3(7)4(8)5(9)10-2/h2-9H,1H2/t2-,3-,4-,5+/m1/s1
InChIKey
HMFHBZSHGGEWLO-AIHAYLRMSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C(C1C(C(C(O1)O)O)O)O
CACTVS 3.341
OC[CH]1O[CH](O)[CH](O)[CH]1O
CACTVS 3.341
OC[C@H]1O[C@H](O)[C@H](O)[C@@H]1O
OpenEye OEToolkits 1.5.0
C([C@@H]1[C@H]([C@H]([C@H](O1)O)O)O)O
ACDLabs 10.04
OC1C(OC(O)C1O)CO
Formula
C5 H10 O5
Name
alpha-D-ribofuranose;
alpha-D-ribose;
D-ribose;
ribose
ChEMBL
CHEMBL606078
DrugBank
ZINC
ZINC000003860714
PDB chain
2kqd Chain A Residue 1003 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure 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
]
PDB
2kqd
Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose).
Resolution
N/A
Binding residue
(original residue number in PDB)
Y386 R387
Binding residue
(residue number reindexed from 1)
Y24 R25
Annotation score
4
Enzymatic activity
Enzyme Commision number
3.1.-.-
Gene Ontology
Molecular Function
GO:0003906
DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0008408
3'-5' exonuclease activity
Biological Process
GO:0006302
double-strand break repair
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:2kqd
,
PDBe:2kqd
,
PDBj:2kqd
PDBsum
2kqd
PubMed
20098424
UniProt
Q8IW19
|APLF_HUMAN Aprataxin and PNK-like factor (Gene Name=APLF)
[
Back to BioLiP
]