Structure of PDB 4ubu Chain H

Receptor sequence
>4ubuH (length=394) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
HGSMGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGL
HAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQ
QANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDID
LPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQ
APVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQ
ISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAK
VLEKAGMKIGDIDIVEINEAFASVVLSWARVHEPDMDRVNVNGGAIALGH
PVGCTGSRLITTALHELERTDQSLALITMCAGGALSTGTIIERI
3D structure
PDB4ubu FadA5 a Thiolase from Mycobacterium tuberculosis: A Steroid-Binding Pocket Reveals the Potential for Drug Development against Tuberculosis.
ChainH
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C93 H347 C377 G379
Catalytic site (residue number reindexed from 1) C96 H350 C380 G382
Enzyme Commision number 2.3.1.16: acetyl-CoA C-acyltransferase.
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 H S93 L128 Q151 F152 R221 G227 L231 A242 S246 S96 L131 Q154 F155 R224 G230 L234 A245 S249
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:0042802 identical protein binding
Biological Process
GO:0006635 fatty acid beta-oxidation
GO:0006707 cholesterol catabolic process
GO:0008203 cholesterol metabolic process
GO:0010124 phenylacetate catabolic process
GO:0016042 lipid catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ubu, PDBe:4ubu, PDBj:4ubu
PDBsum4ubu
PubMed25482540
UniProtI6XHI4|FADA5_MYCTU Steroid 3-ketoacyl-CoA thiolase (Gene Name=fadA5)

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