Structure of PDB 5tif Chain A Binding Site BS01

Receptor Information
>5tif Chain A (length=182) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GMDTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQ
GLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAAN
AEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFLEEVKKKPQ
WMQDDGIHPNRDAQPFIADWMAKQLQPLVNHD
Ligand information
Ligand IDOCA
InChIInChI=1S/C8H16O2/c1-2-3-4-5-6-7-8(9)10/h2-7H2,1H3,(H,9,10)
InChIKeyWWZKQHOCKIZLMA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)CCCCCCC
OpenEye OEToolkits 1.5.0CCCCCCCC(=O)O
CACTVS 3.341CCCCCCCC(O)=O
FormulaC8 H16 O2
NameOCTANOIC ACID (CAPRYLIC ACID)
ChEMBLCHEMBL324846
DrugBankDB04519
ZINCZINC000001530416
PDB chain5tif Chain A Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5tif Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids.
Resolution0.97 Å
Binding residue
(original residue number in PDB)		D9 S10 L11 G44 N73 R108
Binding residue
(residue number reindexed from 1)		D10 S11 L12 G45 N74 R109
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) S10 G44 N73 D154 H157
Catalytic site (residue number reindexed from 1) S11 G45 N74 D155 H158
Enzyme Commision number 3.1.1.2: arylesterase.
3.1.1.5: lysophospholipase.
3.1.2.14: oleoyl-[acyl-carrier-protein] hydrolase.
3.1.2.2: palmitoyl-CoA hydrolase.
3.4.21.-
Gene Ontology
Molecular Function
GO:0004064 arylesterase activity
GO:0004622 lysophospholipase activity
GO:0008233 peptidase activity
GO:0016297 fatty acyl-[ACP] hydrolase activity
GO:0016298 lipase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0042802 identical protein binding
GO:0047617 fatty acyl-CoA hydrolase activity
GO:0052816 long-chain fatty acyl-CoA hydrolase activity
Biological Process
GO:0006508 proteolysis
GO:0006629 lipid metabolic process
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tif, PDBe:5tif, PDBj:5tif
PDBsum5tif
PubMed29375928
UniProtP0ADA1|TESA_ECOLI Thioesterase 1/protease 1/lysophospholipase L1 (Gene Name=tesA)

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