Structure of PDB 5oln Chain B Binding Site BS01
Receptor Information
>5oln Chain B (length=434) Species:
224308
(Bacillus subtilis subsp. subtilis str. 168) [
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AMRMVDIIIKKQNGKELTTEEIQFFVNGYTDGSIPDYQASALAMAIFFQD
MSDRERADLTMAMVNSGETIDLSAIEGIKVDKHSTGGVGDTTTLVLAPLV
AALDVPVAKMSGRGLGHTGGTIDKLEAIMGFHVELTKDEFIKLVNRDKVA
VIGQSGNLTPADKKLYALRDVTGTVNSIPLIASSIMSKKIAAGADAIVLD
VKTGAGAFMKTEEDAAELAKAMVRIGNNVGRQTMAVISDMSQPLGFAIGN
ALEVKEAIDTLKGEGPEDLHELVLTLGSQMVVLAKKADTLDEARAKLEEV
MKNGKALEKFKDFLKNQGGDSSIVDDPSKLPQAAYQIDVPAKEAGVVSEI
VADEIGVAAMLLGAGRATKEDEIDLAVGIMLRKKVGDKVEKGEPLVTLYA
NRENVDEVIAKVYDNIRIAAEAKAPKLIHTLITE
Ligand information
Ligand ID
IMD
InChI
InChI=1S/C3H4N2/c1-2-5-3-4-1/h1-3H,(H,4,5)/p+1
InChIKey
RAXXELZNTBOGNW-UHFFFAOYSA-O
SMILES
Software
SMILES
CACTVS 3.341
[nH]1cc[nH+]c1
ACDLabs 10.04
c1c[nH+]cn1
OpenEye OEToolkits 1.5.0
c1c[nH+]c[nH]1
Formula
C3 H5 N2
Name
IMIDAZOLE
ChEMBL
DrugBank
ZINC
PDB chain
5oln Chain B Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
5oln
Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate.
Resolution
1.88 Å
Binding residue
(original residue number in PDB)
Y165 R168 I180 S183
Binding residue
(residue number reindexed from 1)
Y166 R169 I181 S184
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H82 D161 R168 S183 K187
Catalytic site (residue number reindexed from 1)
H83 D162 R169 S184 K188
Enzyme Commision number
2.4.2.2
: pyrimidine-nucleoside phosphorylase.
Gene Ontology
Molecular Function
GO:0004645
1,4-alpha-oligoglucan phosphorylase activity
GO:0004850
uridine phosphorylase activity
GO:0009032
thymidine phosphorylase activity
GO:0016154
pyrimidine-nucleoside phosphorylase activity
GO:0016757
glycosyltransferase activity
GO:0016763
pentosyltransferase activity
GO:0046872
metal ion binding
GO:0047847
deoxyuridine phosphorylase activity
Biological Process
GO:0006206
pyrimidine nucleobase metabolic process
GO:0006213
pyrimidine nucleoside metabolic process
Cellular Component
GO:0005829
cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5oln
,
PDBe:5oln
,
PDBj:5oln
PDBsum
5oln
PubMed
29633966
UniProt
P39142
|PDP_BACSU Pyrimidine-nucleoside phosphorylase (Gene Name=pdp)
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