Structure of PDB 2w22 Chain A

Receptor sequence
>2w22A (length=388) Species: 33938 (Geobacillus thermocatenulatus) [Search protein sequence]
ASPRANDAPIVLLHGFTGWGREEMLGFKYWGGVRGDIEQWLNDNGYRTYT
LAVGPLSSNWDRACEAYAQLVGGTVDYGAAHAAKHGHARFGRTYPGLLPE
LKRGGRVHIIAHSQGGQTARMLVSLLENGSQEEREYAKAHNVSLSPLFEG
GHHFVLSVTTIATPHDGTTLVNMVDFTDRFFDLQKAVLKAAAVASNVPYT
SQVYDFKLDQWGLRRQPGESFDHYFERLKRSPVWTSTDTARYDLSIPGAE
KLNQWVQASPNTYYLSFSTERTHRGALTGNYYPELGMNAFSAVVCAPFLG
SYRNEALGIDDRWLENDGIVNTVSMNGPKRGSSDRIVPYDGTLKKGVWND
MGTYNVDHLEVIGVDPNPSFDIRAFYLRLAEQLASLRP
3D structure
PDB2w22 Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.1.3: triacylglycerol lipase.
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 CA A G287 E361 D366 P367 G286 E360 D365 P366
BS02 ZN A D62 H82 H88 D239 D61 H81 H87 D238
BS03 EGC A F17 L57 S114 L184 Q185 V188 L189 T240 F16 L56 S113 L183 Q184 V187 L188 T239
BS04 EGC A T178 L360 T177 L359
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:2w22, PDBe:2w22, PDBj:2w22
PDBsum2w22
PubMed19056729
UniProtQ59260

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