BioLiP

Receptor Information

>3hle Chain A (length=424) Species: 33178 (Aspergillus terreus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

HHSSGLVPRGSHMGSIIDAAAAAGPVVLMETAFRKAVESRQIPGAVIMAR
DASGNLNYTRCFGARTVRRDENNQLPPLQVDTPCRLAAATKLLTTIMVLQ
CMERGLVDLDETVDRLLPDLSAMPVLEGFDDAGNARLRERRGKITLRHLL
THTSGLSYVFLHPLLREYMAQGYLQSAEKFGIQSRLAPPAVNDPGAEWIY
GTNLDWAGKLVERATGLDLEQYLQENICAPLGITDMTFKLQQRPDMLARR
ADQTHRNSADGRLRYDDSVYFRADGEECFGGQGVFSSPGSYMKVLHSLLK
RDGLLLQPQTVDLMFQPALEPRLEEQMNQHMDASPHINYGGPMPMVLRRS
FGLGGIIALEDLDGENWRRKGSLTFGGGPNIVWQIDPKAGLCTLAFFQLE
PWNDPVCRDLTRTFEHAIYAQYQQ

Ligand ID

MJA

InChI

InChI=1S/C19H30O5/c1-11-7-13-4-3-12(2)16(19(13)17(22)8-11)6-5-14(20)9-15(21)10-18(23)24/h3-4,7,11-12,14-17,19-22H,5-6,8-10H2,1-2H3,(H,23,24)/t11-,12-,14+,15+,16-,17-,19-/m0/s1

InChIKey

FJQFRDAWQRBFCG-IRUSZSJRSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	CC1CC(C2C(C(C=CC2=C1)C)CCC(CC(CC(=O)O)O)O)O
ACDLabs 10.04	O=C(O)CC(O)CC(O)CCC2C(C=CC1=CC(CC(O)C12)C)C
OpenEye OEToolkits 1.5.0	C[C@@H]1C[C@@H]([C@@H]2[C@H]([C@H](C=CC2=C1)C)CC[C@H](C[C@H](CC(=O)O)O)O)O
CACTVS 3.341	C[CH]1C[CH](O)[CH]2[CH](CC[CH](O)C[CH](O)CC(O)=O)[CH](C)C=CC2=C1
CACTVS 3.341	C[C@@H]1C[C@H](O)[C@@H]2[C@@H](CC[C@@H](O)C[C@@H](O)CC(O)=O)[C@@H](C)C=CC2=C1

Formula

C19 H30 O5

Name

(3R,5R)-3,5-dihydroxy-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]heptanoic acid;
Monacolin J acid

PDB chain

3hle Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	3hle Directed evolution and structural characterization of a simvastatin synthase
Resolution	2.06 Å
Binding residue (original residue number in PDB)	F148 Y188 I325 F363 E388 W390
Binding residue (residue number reindexed from 1)	F160 Y200 I337 F375 E400 W402
Annotation score	5

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.

	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

PDB	RCSB:3hle, PDBe:3hle, PDBj:3hle
PDBsum	3hle
PubMed	19875080
UniProt	Q9Y7D1\|LOVD_ASPTE Monacolin J acid methylbutanoyltransferase (Gene Name=lovD)

[Back to BioLiP]

Structure of PDB 3hle Chain A Binding Site BS01