Structure of PDB 6pcd Chain A

Receptor sequence
>6pcdA (length=401) Species: 160488 (Pseudomonas putida KT2440) [Search protein sequence]
HQGSMHDVFICDAIRTPIGRFGGALASVRADDLAAVPLKALIERNPGVQW
DQVDEVFFGCANQAGEDNRNVARMALLLAGLPESIPGVTLNRLSASGMDA
VGTAFRAIASGEMELVIAGGVESMSRAPFVMGKAESAYSRNMKLEDTTIG
WRFINPLMKSQYGVDSMPETADNVADDYQVSRADQDAFALRSQQKAAAAQ
AAGFFAEEIVPVRIAHEIIVERDEHLRPETTLEALTKLKPVNGPDKTVTA
GNASGVNDGAAAMILASAAAVKKHGLTPRARVLGMASGGVAPRVMGIGPV
PAVRKLTERLGIAVSDFDVIELNEAFASQGLAVLRELGVADDAPQVNPNG
GAIALGAPLGMSGARLVLTALHQLEKSGGRKGLATMCVGVGQGLALAIER
V
3D structure
PDB6pcd Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.
ChainA
Resolution1.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S90 A356 C386 G388
Catalytic site (residue number reindexed from 1) S94 A357 C387 G389
Enzyme Commision number 2.3.1.174: 3-oxoadipyl-CoA thiolase.
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 COA A I145 M163 R226 T229 A249 S253 G254 A324 A356 I149 M167 R227 T230 A250 S254 G255 A325 A357
BS02 OYA A N58 T143 T144 I145 G146 R148 L358 N62 T147 T148 I149 G150 R152 L359
Gene Ontology
Molecular Function
GO:0003988 acetyl-CoA C-acyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0033812 3-oxoadipyl-CoA thiolase activity
Biological Process
GO:0006635 fatty acid beta-oxidation
GO:0010124 phenylacetate catabolic process
GO:0019619 3,4-dihydroxybenzoate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6pcd, PDBe:6pcd, PDBj:6pcd
PDBsum6pcd
PubMed32647822
UniProtQ88N39

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