Structure of PDB 1u8u Chain A

Receptor sequence

>1u8uA (length=178) Species: 562 (Escherichia coli)

ADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQG
LARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAANA
EPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFMEEVYLKPQW
MQDDGIHPNRDAQPFIADWMAKQLQPLV

3D structure

• PDB: 1u8u Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement
• Chain: A
• Resolution: 2.08 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S10 G44 N73 D154 H157
• Catalytic site (residue number reindexed from 1): S10 G44 N73 D154 H157
• 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	SO4	A	M17 S18 K34 T35 R160 Q175	M17 S18 K34 T35 R160 Q175
BS02	OCA	A	D9 S10 G44 G72 N73 R108 P110 H157	D9 S10 G44 G72 N73 R108 P110 H157

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:1u8u, PDBe:1u8u, PDBj:1u8u
• PDBsum: 1u8u
• PubMed: 15697222
• UniProt: P0ADA1|TESA_ECOLI Thioesterase 1/protease 1/lysophospholipase L1 (Gene Name=tesA)