Structure of PDB 2dsn Chain A Binding Site BS02

Receptor Information

>2dsn Chain A (length=387) Species: 213419 (Geobacillus zalihae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SLRANDAPIVLLHGFTGWGREEMFGFKYWGGVRGDIEQWLNDNGYRTYTL
AVGPLSSNWDRACEAYAQLVGGTVDYGAAHAAKHGHARFGRTYPGLLPEL
KRGGRIHIIAHSQGGQTARMLVSLLENGSQEEREYAKAHNVSLSPLFEGG
HHFVLSVTTIATPHDGTTLVNMVDFTDRFFDLQKAVLEAAAVASNVPYTS
QVYDFKLDQWGLRRQPGESFDHYFERLKRSPVWTSTDTARYDLSVSGAEK
LNQWVQASPNTYYLSFSTERTYRGALTGNHYPELGMNAFSAVVCAPFLGS
YRNPTLGIDDRWLENDGIVNTVSMNGPKRGSSDRIVPYDGTLKKGVWNDM
GTYNVDHLEIIGVDPNPSFDIRAFYLRLAEQLASLQP

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

2dsn Chain A Residue 2011 [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	2dsn Novel cation-pi interaction revealed by crystal structure of thermoalkalophilic lipase
Resolution	1.5 Å
Binding residue (original residue number in PDB)	G286 E360 D365 P366
Binding residue (residue number reindexed from 1)	G285 E359 D364 P365
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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Cellular Component

External links

PDB	RCSB:2dsn, PDBe:2dsn, PDBj:2dsn
PDBsum	2dsn
PubMed	17932933
UniProt	Q842J9

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