Structure of PDB 3hle Chain A

Receptor sequence
>3hleA (length=424) Species: 33178 (Aspergillus terreus) [Search protein sequence]
HHSSGLVPRGSHMGSIIDAAAAAGPVVLMETAFRKAVESRQIPGAVIMAR
DASGNLNYTRCFGARTVRRDENNQLPPLQVDTPCRLAAATKLLTTIMVLQ
CMERGLVDLDETVDRLLPDLSAMPVLEGFDDAGNARLRERRGKITLRHLL
THTSGLSYVFLHPLLREYMAQGYLQSAEKFGIQSRLAPPAVNDPGAEWIY
GTNLDWAGKLVERATGLDLEQYLQENICAPLGITDMTFKLQQRPDMLARR
ADQTHRNSADGRLRYDDSVYFRADGEECFGGQGVFSSPGSYMKVLHSLLK
RDGLLLQPQTVDLMFQPALEPRLEEQMNQHMDASPHINYGGPMPMVLRRS
FGLGGIIALEDLDGENWRRKGSLTFGGGPNIVWQIDPKAGLCTLAFFQLE
PWNDPVCRDLTRTFEHAIYAQYQQ
3D structure
PDB3hle Directed evolution and structural characterization of a simvastatin synthase
ChainA
Resolution2.06 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A76 K79 Y146 F148 Y188 D193 N245 F363 G366
Catalytic site (residue number reindexed from 1) A88 K91 Y158 F160 Y200 D205 N257 F375 G378
Enzyme Commision number 2.3.1.238: monacolin J acid methylbutanoate transferase.
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 MJA A F148 Y188 I325 F363 E388 W390 F160 Y200 I337 F375 E400 W402
Gene Ontology
Molecular Function
GO:0016218 polyketide synthase activity
GO:0016746 acyltransferase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:0030639 polyketide biosynthetic process
GO:0050832 defense response to fungus
GO:0140735 lovastatin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3hle, PDBe:3hle, PDBj:3hle
PDBsum3hle
PubMed19875080
UniProtQ9Y7D1|LOVD_ASPTE Monacolin J acid methylbutanoyltransferase (Gene Name=lovD)

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