Structure of PDB 4lrt Chain A Binding Site BS01

Receptor Information
>4lrt Chain A (length=334) Species: 471852 (Thermomonospora curvata DSM 43183) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APRVRITDSTLRDGSHAMAHQFTEEQVRATVHALDAAGVEVIEVSHGDGL
GGSSFNYGFSAVDEIDLVAAAVDEAVNAKIAVLLLPGVGTVRDLKRAHDA
GASVARIATHCTEADVSCQHFAAARELGMETVGFLMLAHRIGPEELARQA
RIMVDAGAQCVYVVDSAGALVLSDVQARVQALVREIGHEAQVGFHGHQNL
SLGVANSVLAYQNGARQIDGALCALGAGAGNSPTEILAATFERLNIETGV
NVQAALAAAEEVVRPYLPRLPWADRAAIVQGYAGVYSSFLLHAERAAERY
GVPAHEILQRVGEAGYVGGQEDMIIDIAVQLAEE
Ligand information
Ligand IDPYR
InChIInChI=1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6)
InChIKeyLCTONWCANYUPML-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(=O)C(O)=O
OpenEye OEToolkits 1.7.6CC(=O)C(=O)O
ACDLabs 12.01O=C(C(=O)O)C
FormulaC3 H4 O3
NamePYRUVIC ACID
ChEMBLCHEMBL1162144
DrugBankDB00119
ZINCZINC000001532517
PDB chain4lrt Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4lrt Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
Resolution1.5 Å
Binding residue
(original residue number in PDB)		R21 D22 M145 V173 S175 H204 Y295
Binding residue
(residue number reindexed from 1)		R12 D13 M136 V164 S166 H195 Y286
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D22 H25 H204 H206 Y295
Catalytic site (residue number reindexed from 1) D13 H16 H195 H197 Y286
Enzyme Commision number 4.1.3.39: 4-hydroxy-2-oxovalerate aldolase.
4.1.3.43: 4-hydroxy-2-oxohexanoate aldolase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003852 2-isopropylmalate synthase activity
GO:0008701 4-hydroxy-2-oxovalerate aldolase activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process
GO:0009098 L-leucine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4lrt, PDBe:4lrt, PDBj:4lrt
PDBsum4lrt
PubMed
UniProtD1A3K8

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