Structure of PDB 6pcc Chain A

Receptor sequence
>6pccA (length=403) Species: 160488 (Pseudomonas putida KT2440) [Search protein sequence]
QGSMHDVFICDAIRTPIGRFGGALASVRADDLAAVPLKALIERNPGVQWD
QVDEVFFGCANQAGEDNRNVARMALLLAGLPESIPGVTLNRLCASGMDAV
GTAFRAIASGEMELVIAGGVESMSRAPFVMGKAESAYSRNMKLEDTTIGW
RFINPLMKSQYGVDSMPETADNVADDYQVSRADQDAFALRSQQKAAAAQA
AGFFAEEIVPVRIAHKKGEIIVERDEHLRPETTLEALTKLKPVNGPDKTV
TAGNASGVNDGAAAMILASAAAVKKHGLTPRARVLGMASGGVAPRVMGIG
PVPAVRKLTERLGIAVSDFDVIELNEAFASQGLAVLRELGVADDAPQVNP
NGGAIALGAPLGMSGARLVLTALHQLEKSGGRKGLATMCVGVGQGLALAI
ERV
3D structure
PDB6pcc Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.
ChainA
Resolution1.96 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C90 A356 C386 G388
Catalytic site (residue number reindexed from 1) C93 A359 C389 G391
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 C90 I145 R226 T229 A249 S253 N322 F325 C93 I148 R229 T232 A252 S256 N325 F328
BS02 O8Y A N58 T143 I145 G146 R148 L358 N61 T146 I148 G149 R151 L361
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:6pcc, PDBe:6pcc, PDBj:6pcc
PDBsum6pcc
PubMed32647822
UniProtQ88N39

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