Structure of PDB 4moc Chain A

Receptor sequence
>4mocA (length=273) Species: 9606 (Homo sapiens) [Search protein sequence]
MGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTAS
VDDIQFEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGIEKLVS
VAFSTFVAKPVGKEKIHLKPVTLLTEQDHVEHNLAAERRKVRLQHEDTRG
TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSV
DMFKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWAEGRGRH
INSAFLIYNAADDKENLITFPRI
3D structure
PDB4moc Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain.
ChainA
Resolution2.5 Å
3D
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
Enzyme Commision number 3.1.2.1: acetyl-CoA hydrolase.
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 V52 T53 S55 S82 T83 S84 T110 R144 E151 T200 I205 K234 F235 G237 V47 T48 S50 S77 T78 S79 T105 R139 E146 T170 I175 K204 F205 G207
Gene Ontology
Molecular Function
GO:0016790 thiolester hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4moc, PDBe:4moc, PDBj:4moc
PDBsum4moc
PubMed25002576
UniProtQ8WYK0|ACO12_HUMAN Acetyl-coenzyme A thioesterase (Gene Name=ACOT12)

[Back to BioLiP]