Structure of PDB 3vpd Chain B Binding Site BS02
Receptor Information
>3vpd Chain B (length=268) Species:
274
(Thermus thermophilus) [
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MLAILYDRIRPDERMLFERAEALGLPYKKVYVPALPMVLGERPEALEGVT
VALERCVSQSRGLAAARYLTALGIPVVNRPEVIEACGDKWATSVALAKAG
LPQPKTALATDREEALRLMEAFGYPVVLKPVIGSWGRLLAKVTDRAAAEA
LLEHKEVLGGFQHQLFYIQEYVEKPGRDIRVFVVGERAIAAIYRQAENCP
LTEEIARLSVGAAEAVGGGVVAVDLFESERGLLVNEVNHTMEFKNSVHTT
GVDIPGEILRYAWEVARG
Ligand information
Ligand ID
BUA
InChI
InChI=1S/C4H8O2/c1-2-3-4(5)6/h2-3H2,1H3,(H,5,6)
InChIKey
FERIUCNNQQJTOY-UHFFFAOYSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 2.0.7
CCCC(=O)O
CACTVS 3.385
CCCC(O)=O
Formula
C4 H8 O2
Name
butanoic acid
ChEMBL
CHEMBL14227
DrugBank
DB03568
ZINC
ZINC000000895132
PDB chain
3vpd Chain B Residue 302 [
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Receptor-Ligand Complex Structure
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PDB
3vpd
Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
Resolution
1.95 Å
Binding residue
(original residue number in PDB)
F256 K257 N258 S259
Binding residue
(residue number reindexed from 1)
F243 K244 N245 S246
Annotation score
1
Enzymatic activity
Enzyme Commision number
6.3.2.43
: [amino-group carrier protein]--L-2-aminoadipate ligase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0005524
ATP binding
GO:0016874
ligase activity
GO:0018169
ribosomal S6-glutamic acid ligase activity
GO:0046872
metal ion binding
Biological Process
GO:0009085
lysine biosynthetic process
GO:0009432
SOS response
GO:0018410
C-terminal protein amino acid modification
GO:0019878
lysine biosynthetic process via aminoadipic acid
GO:0036211
protein modification process
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3vpd
,
PDBe:3vpd
,
PDBj:3vpd
PDBsum
3vpd
PubMed
23434852
UniProt
Q5SH23
|LYSX_THET8 Alpha-aminoadipate--LysW ligase LysX (Gene Name=lysX)
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