Structure of PDB 7dbl Chain C

Receptor sequence
>7dblC (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.
ChainC
Resolution1.84 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 C V60 A139 F140 L165 Q167 P171 I183 Q265 R301 F327 H365 V58 A137 F138 L163 Q165 P169 I181 Q263 R299 F325 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
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')

[Back to BioLiP]