Structure of PDB 1esp Chain A Binding Site BS03

Receptor Information

>1esp Chain A (length=317) Species: 1396 (Bacillus cereus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

VTGTNKVGTGKGVLGDTKSLNTTLSGSSYYLQDNTRGATIFTYDAKNRST
LPGTLWADADNVFNAAYDAAAVDAHYYAGKTYDYYKATFNRNSINDAGAP
LKSTVHYGSNYNNAFWNGSQMVYGDGDGVTFTSLSGGIDVIGHSLTHAVT
ENSSNLIYQNESGALNEAISDIFGTLVEFYDNRNPDWEIGEDIYTPGKAG
DALRSMSDPTKYGDPDHYSKRYTGSSDNGGVHTNSGIINKQAYLLANGGT
HYGVTVTGIGKDKLGAIYYRANTQYFTQSTTFSQARAGAVQAAADLYGAN
SAEVAAVKQSFSAVGVN

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

1esp Chain A Residue 321 [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	1esp E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution.
Resolution	2.8 Å
Binding residue (original residue number in PDB)	D58 D60 V62
Binding residue (residue number reindexed from 1)	D58 D60 V62
Annotation score	4

Enzymatic activity

Catalytic site (original residue number in PDB)	H143 S144 H147 Y158 E167 D227 H232
Catalytic site (residue number reindexed from 1)	H143 S144 H147 Y158 E167 D227 H232
Enzyme Commision number	3.4.24.28: bacillolysin.

Gene Ontology

	Molecular Function
GO:0004222	metalloendopeptidase activity

	Biological Process
GO:0006508	proteolysis

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Molecular Function

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Biological Process

External links

PDB	RCSB:1esp, PDBe:1esp, PDBj:1esp
PDBsum	1esp
PubMed	15299677
UniProt	P05806\|NPRE_BACCE Bacillolysin (Gene Name=npr)

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