Structure of PDB 7dbl Chain B

Receptor sequence
>7dblB (length=418) Species: 5074 (Penicillium brevicompactum) [Search protein sequence]
TEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAI
TFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNE
DKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHAFGGNIITNLAYLH
PRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRA
NRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPV
TLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRP
EPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPD
GRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRD
GKSHLAVEENWYKVLKPI
3D structure
PDB7dbl Structural basis for substrate specificity of the peroxisomal acyl-CoA hydrolase MpaH' involved in mycophenolic acid biosynthesis.
ChainB
Resolution1.84 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.1.-
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 MOA B G59 V60 A139 F140 L165 Q167 P171 I183 Q265 R301 F327 L328 H365 G57 V58 A137 F138 L163 Q165 P169 I181 Q263 R299 F325 L326 H363
Gene Ontology
Molecular Function
GO:0016218 polyketide synthase activity
GO:0016787 hydrolase activity
GO:0047617 fatty acyl-CoA hydrolase activity
Biological Process
GO:0016114 terpenoid biosynthetic process
GO:0017000 antibiotic biosynthetic process
GO:0072330 monocarboxylic acid biosynthetic process
GO:0140722 mycophenolic acid biosynthetic process
Cellular Component
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7dbl, PDBe:7dbl, PDBj:7dbl
PDBsum7dbl
PubMed33843134
UniProtA0A0B5LB55|MPAH2_PENBR Type I acyl-CoA thioesterase mpaH' (Gene Name=mpaH')

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