Structure of PDB 5c0q Chain A Binding Site BS02

Receptor Information

>5c0q Chain A (length=450) Species: 2337 (Thermotoga neapolitana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

DLGKLFFCGFDDFNEEAREVIQKYRPAGVLIYPGVLSKEYLFLDFMNFLS
RNGRFIVSSDHEGGQLEVLKYVPSFPGNLAAGKVDPVFTGRYCEMAGRIM
NTLGFNMVFAPVLDLLSELRSFGSDPEVVASHGMEACMGYFKGGVIPCIK
HFPGHGKTADDSHYLLPTVNASFEELWREDLLPFRRIFQSRVKTAVMTAH
VKYPAVDDLPATLSKKLITEVLREKLNFKGLVLSDAMEMKAISENFSVEE
AVRFFIEAGGNMILLDNFRDLPVYYESLKKLIEDGSIERGKVERSIKIVD
EYLSALENRFNSGLIAEVAERAIECTRMRKELLGREVVLLVPSNTTGDDY
DLIPEVAKRFFKVRDVIRYDIEAGPDDVDGELIFDFVVNASKNEQVLQAH
LSLPSDRTIYFIIRNPFDAKFFPGRSVVITHSTKPISVYKSFQHLLGRCS

Ligand information

Ligand ID

InChI

InChI=1S/Zn/q+2

InChIKey

PTFCDOFLOPIGGS-UHFFFAOYSA-N

SMILES

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

Formula

Name

ZINC ION

PDB chain

5c0q Chain A Residue 1002 [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	5c0q Crystal structure of beta-N-acetylglucosaminidase CbsA from Thermotoga neapolitana
Resolution	2.499 Å
Binding residue (original residue number in PDB)	D171 H173
Binding residue (residue number reindexed from 1)	D161 H163
Annotation score	4

Enzymatic activity

Enzyme Commision number

3.2.1.52: beta-N-acetylhexosaminidase.

Gene Ontology

	Molecular Function
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016787	hydrolase activity
GO:0046872	metal ion binding

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0009254	peptidoglycan turnover

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Molecular Function

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Biological Process

External links

PDB	RCSB:5c0q, PDBe:5c0q, PDBj:5c0q
PDBsum	5c0q
PubMed	26187666
UniProt	Q9AG27

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