8VZC

Crystal Structure of 2-Hydroxyacyl-CoA Lyase/Synthse ApbHACS from Alphaproteobacteria bacterium in the Complex with THDP, Formyl-CoA, and ADP

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001561	biological_process	fatty acid alpha-oxidation
A	0005777	cellular_component	peroxisome
A	0008949	molecular_function	oxalyl-CoA decarboxylase activity
A	0016829	molecular_function	lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030976	molecular_function	thiamine pyrophosphate binding
B	0001561	biological_process	fatty acid alpha-oxidation
B	0005777	cellular_component	peroxisome
B	0008949	molecular_function	oxalyl-CoA decarboxylase activity
B	0016829	molecular_function	lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0030976	molecular_function	thiamine pyrophosphate binding
C	0001561	biological_process	fatty acid alpha-oxidation
C	0005777	cellular_component	peroxisome
C	0008949	molecular_function	oxalyl-CoA decarboxylase activity
C	0016829	molecular_function	lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0030976	molecular_function	thiamine pyrophosphate binding
D	0001561	biological_process	fatty acid alpha-oxidation
D	0005777	cellular_component	peroxisome
D	0008949	molecular_function	oxalyl-CoA decarboxylase activity
D	0016829	molecular_function	lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0030976	molecular_function	thiamine pyrophosphate binding

Functional Information from PROSITE/UniProt

site_id	PS00187
Number of Residues	20
Details	TPP_ENZYMES Thiamine pyrophosphate enzymes signature. VAaaavhPgrpvIaVqGDSA

Chain	Residue	Details
A	VAL428-ALA447

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