Structure of PDB 4lrt Chain A

Receptor sequence

>4lrtA (length=334) Species: 471852 (Thermomonospora curvata DSM 43183)

APRVRITDSTLRDGSHAMAHQFTEEQVRATVHALDAAGVEVIEVSHGDGL
GGSSFNYGFSAVDEIDLVAAAVDEAVNAKIAVLLLPGVGTVRDLKRAHDA
GASVARIATHCTEADVSCQHFAAARELGMETVGFLMLAHRIGPEELARQA
RIMVDAGAQCVYVVDSAGALVLSDVQARVQALVREIGHEAQVGFHGHQNL
SLGVANSVLAYQNGARQIDGALCALGAGAGNSPTEILAATFERLNIETGV
NVQAALAAAEEVVRPYLPRLPWADRAAIVQGYAGVYSSFLLHAERAAERY
GVPAHEILQRVGEAGYVGGQEDMIIDIAVQLAEE

3D structure

• PDB: 4lrt 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
• Chain: A
• Resolution: 1.5 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	PYR	A	R21 D22 M145 V173 S175 H204 Y295	R12 D13 M136 V164 S166 H195 Y286
BS02	MG	A	D22 H204 H206	D13 H195 H197

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

External links

• PDB: RCSB:4lrt, PDBe:4lrt, PDBj:4lrt
• PDBsum: 4lrt
• UniProt: D1A3K8