Structure of PDB 7dbl Chain D

Receptor sequence
>7dblD (length=420) Species: 5074 (Penicillium brevicompactum) [Search protein sequence]
MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKRVPDDAIT
FIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNED
KLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHAFGGNIITNLAYLHP
RLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRAN
RAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVT
LTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPE
PRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDG
RVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDG
KSHLAVEENWYKVLKPIPSG
3D structure
PDB7dbl Structural basis for substrate specificity of the peroxisomal acyl-CoA hydrolase MpaH' involved in mycophenolic acid biosynthesis.
ChainD
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 D G59 V60 A139 F140 Q167 P171 Q265 R301 P304 F327 H365 G56 V57 A136 F137 Q164 P168 Q262 R298 P301 F324 H362
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]