Structure of PDB 6pcb Chain C

Receptor sequence
>6pcbC (length=397) Species: 160488 (Pseudomonas putida KT2440) [Search protein sequence]
SMHDVFICDAIRTPIGRFGGALASVRADDLAAVPLKALIERNPGVQWDQV
DEVFFGCANQAGEDNRNVARMALLLAGLPESIPGVTLNRLCASGMDAVGT
AFRAIASGEMELVIAGGVESMSRAPFVMGKAESAYSRNMKLEDTTIGWRF
INPLMKSQYGVDSMPETADNVADDYQVSRADQDAFALRSQQKAAAAQAAG
FFAEEIVPVRIAEIIVERDEHLRPETTLEALTKLKPVNGPDKTVTAGNAS
GVNDGAAAMILASAAAVKKHGLTPRARVLGMASGGVAPRVMGIGPVPAVR
KLTERLGIAVSDFDVIELNEAFASQGLAVLRELGVADDAPQVNPNGGAIA
LGAPLGMSGARLVLTALHQLEKSGGRKGLATMCVGVGQGLALAIERV
3D structure
PDB6pcb Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.
ChainC
Resolution1.61 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) C90 A356 C386 G388
Catalytic site (residue number reindexed from 1) C91 A353 C383 G385
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 C C90 I145 R226 A249 S253 N322 F325 C91 I146 R223 A246 S250 N319 F322
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6pcb, PDBe:6pcb, PDBj:6pcb
PDBsum6pcb
PubMed32647822
UniProtQ88N39

[Back to BioLiP]