Structure of PDB 1ku0 Chain A Binding Site BS02

Receptor Information

>1ku0 Chain A (length=388) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ASPRANDAPIVLLHGFTGWGREEMLGFKYWGGVRGDIEQWLNDNGYRTYT
LAVGPLSSNWDRACEAYAQLVGGTVDYGAAHAAKHGHARFGRTYPGLLPE
LKRGGRVHIIAHSQGGQTARMLVSLLENGSQEEREYAKEHNVSLSPLFEG
GHRFVLSVTTIATPHDGTTLVNMVDFTDRFFDLQKAVLEAAAVASNAPYT
SEIYDFKLDQWGLRREPGESFDHYFERLKRSPVWTSTDTARYDLSVPGAE
TLNRWVKASPNTYYLSFSTERTYRGALTGNYYPELGMNAFSAIVCAPFLG
SYRNAALGIDSHWLGNDGIVNTISMNGPKRGSNDRIVPYDGTLKKGVWND
MGTYNVDHLEVIGVDPNPSFNIRAFYLRLAEQLASLRP

Ligand information

Ligand ID

InChI

InChI=1S/Ca/q+2

InChIKey

BHPQYMZQTOCNFJ-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341	[Ca++]
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Ca+2]

Formula

Name

CALCIUM ION

PDB chain

1ku0 Chain A Residue 703 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1ku0 Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase.
Resolution	2.0 Å
Binding residue (original residue number in PDB)	G286 E360 D365 P366
Binding residue (residue number reindexed from 1)	G286 E360 D365 P366
Annotation score	1

Enzymatic activity

Enzyme Commision number

3.1.1.3: triacylglycerol lipase.

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:1ku0, PDBe:1ku0, PDBj:1ku0
PDBsum	1ku0
PubMed	11859083
UniProt	O66015

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