Structure of PDB 1npc Chain A Binding Site BS03

Receptor Information
>1npc 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
LKSTVHYGSNYNNAFWNGSQMVYGDGDGVTFTSLSGGIDVIGHELTHAVT
ENSSNLIYQNESGALNEAISDIFGTLVEFYDNRNPDWEIGEDIYTPGKAG
DALRSMSDPTKYGDPDHYSKRYTGSSDNGGVHTNSGIINKQAYLLANGGT
HYGVTVTGIGKDKLGAIYYRANTQYFTQSTTFSQARAGAVQAAADLYGAN
SAEVAAVKQSFSAVGVN
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1npc Chain A Residue 321 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1npc The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D58 D60 V62
Binding residue
(residue number reindexed from 1)		D58 D60 V62
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H143 E144 H147 Y158 E167 D227 H232
Catalytic site (residue number reindexed from 1) H143 E144 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1npc, PDBe:1npc, PDBj:1npc
PDBsum1npc
PubMed1633827
UniProtP05806|NPRE_BACCE Bacillolysin (Gene Name=npr)

[Back to BioLiP]