Structure of PDB 2vl1 Chain A Binding Site BS04
Receptor Information
>2vl1 Chain A (length=433) Species:
4934
(Lachancea kluyveri) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
PLSIASGRLNQTILETGSQFGGVARWGQESHEFGMRRLAGTALDGAMRDW
FTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDTQPEAGKYDG
ILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSH
DLSLEEAYGLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEIDAHFELH
IEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALL
MSSKMIVAASEIAQRHNGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSD
DVLATMLKEAAAEFDRLIKINDGGALSYESETLQVSPAVNFHEVCIECVS
RSAFAQFKKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEY
SSPEEIENGFKVLLQAIINYDNYRVIRGHQFPG
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
2vl1 Chain A Residue 501 [
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
2vl1
A Recruited Protease is Involved in Catabolism of Pyrimidines.
Resolution
2.15 Å
Binding residue
(original residue number in PDB)
D125 E160 H421
Binding residue
(residue number reindexed from 1)
D99 E134 H395
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.5.1.6
: beta-ureidopropionase.
Gene Ontology
Molecular Function
GO:0003837
beta-ureidopropionase activity
GO:0016787
hydrolase activity
GO:0016813
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872
metal ion binding
View graph for
Molecular Function
External links
PDB
RCSB:2vl1
,
PDBe:2vl1
,
PDBj:2vl1
PDBsum
2vl1
PubMed
18448119
UniProt
Q96W94
[
Back to BioLiP
]