Structure of PDB 5tif Chain A

Receptor sequence

>5tifA (length=182) Species: 562 (Escherichia coli)

GMDTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQ
GLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAAN
AEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFLEEVKKKPQ
WMQDDGIHPNRDAQPFIADWMAKQLQPLVNHD

3D structure

• PDB: 5tif Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids.
• Chain: A
• Resolution: 0.97 Å

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.-

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	OCA	A	D9 S10 L11 G44 N73 R108	D10 S11 L12 G45 N74 R109

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

External links

• PDB: RCSB:5tif, PDBe:5tif, PDBj:5tif
• PDBsum: 5tif
• PubMed: 29375928
• UniProt: P0ADA1|TESA_ECOLI Thioesterase 1/protease 1/lysophospholipase L1 (Gene Name=tesA)