Structure of PDB 4jn6 Chain A

Receptor sequence

>4jn6A (length=338) Species: 1773 (Mycobacterium tuberculosis)

MWDVRITDTSLRDGSHHKRHQFTKDEVGAIVAALDAAGVPVIEVTHGDGL
GGSSFNYGFSKTPEQELIKLAAATAKEARIAFLMLPGVGTKDDIKEARDN
GGSICRIATHCTEADVSIQHFGLARELGLETVGFLMMAHTIAPEKLAAQA
RIMADAGCQCVYVVDSAGALVLDGVADRVSALVAELGEDAQVGFHGHENL
GLGVANSVAAVRAGAKQIDGSCRRFGAGAGNAPVEALIGVFDKIGVKTGI
DFFDIADAAEDVVRPAMPAECLLDRNALIMGYSGVYSSFLKHAVRQAERY
GVPASALLHRAGQRKLIGGQEDQLIDIALEIKRELDSG

3D structure

• PDB: 4jn6 Characterization of an Aldolase-Dehydrogenase Complex from the Cholesterol Degradation Pathway of Mycobacterium tuberculosis.
• Chain: A
• Resolution: 1.93 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D16 H19 H198 H200 Y289
• 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	OXL	A	R15 F137 M139 V167 S169 Y289	R12 F134 M136 V164 S166 Y286
BS02	MN	A	D16 H198 H200	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

Cellular Component

• GO:0009274 peptidoglycan-based cell wall

External links

• PDB: RCSB:4jn6, PDBe:4jn6, PDBj:4jn6
• PDBsum: 4jn6
• PubMed: 23614353
• UniProt: P9WMK5|HOA_MYCTU 4-hydroxy-2-oxohexanoate aldolase (Gene Name=hsaF)