Structure of PDB 6pcc Chain D

Receptor sequence
>6pccD (length=402) Species: 160488 (Pseudomonas putida KT2440) [Search protein sequence]
GSMHDVFICDAIRTPIGRFGGALASVRADDLAAVPLKALIERNPGVQWDQ
VDEVFFGCANQAGEDNRNVARMALLLAGLPESIPGVTLNRLCASGMDAVG
TAFRAIASGEMELVIAGGVESMSRAPFVMGKAESAYSRNMKLEDTTIGWR
FINPLMKSQYGVDSMPETADNVADDYQVSRADQDAFALRSQQKAAAAQAA
GFFAEEIVPVRIAHKKGEIIVERDEHLRPETTLEALTKLKPVNGPDKTVT
AGNASGVNDGAAAMILASAAAVKKHGLTPRARVLGMASGGVAPRVMGIGP
VPAVRKLTERLGIAVSDFDVIELNEAFASQGLAVLRELGVADDAPQVNPN
GGAIALGAPLGMSGARLVLTALHQLEKSGGRKGLATMCVGVGQGLALAIE
RV
3D structure
PDB6pcc Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.
ChainD
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) C92 A358 C388 G390
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 D C90 I145 R226 A249 S253 N322 F325 L358 C92 I147 R228 A251 S255 N324 F327 L360
BS02 O8Y D N58 T143 I145 G146 R148 L358 N60 T145 I147 G148 R150 L360
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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