Structure of PDB 5c0q Chain B

Receptor sequence
>5c0qB (length=457) Species: 2337 (Thermotoga neapolitana) [Search protein sequence]
DVDLGKLFFCGFDDFNEEAREVIQKYRPAGVLIYPGVLSKEYLFLDFMNF
LSRNGRFIVSSDHEGGQLEVLKYVPSFPGNLAAGKVDPVFTGRYCEMAGR
IMNTLGFNMVFAPVLDLLSEKGSVDLRSFGSDPEVVASHGMEACMGYFKG
GVIPCIKHFPGHGKTADDSHYLLPTVNASFEELWREDLLPFRRIFQSRVK
TAVMTAHVKYPAVDDLPATLSKKLITEVLREKLNFKGLVLSDAMEMKAIS
ENFSVEEAVRFFIEAGGNMILLDNFRDLPVYYESLKKLIEDGSIERGKVE
RSIKIVDEYLSALENRFNSGLIAEVAERAIECTRMRKELLGREVVLLVPS
NTTGDDYDLIPEVAKRFFKVRDVIRYDIEAGPDDVDGELIFDFVVNASKN
EQVLQAHLSLPSDRTIYFIIRNPFDAKFFPGRSVVITHSTKPISVYKSFQ
HLLGRCS
3D structure
PDB5c0q Crystal structure of beta-N-acetylglucosaminidase CbsA from Thermotoga neapolitana
ChainB
Resolution2.499 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN B E334 H448 E331 H438
BS02 ZN B D117 H161 H165 D116 H158 H162
BS03 ZN B D171 H173 D168 H170
BS04 ZN B E327 E330 E324 E327
BS05 ZN B E346 E398 E343 E388
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
PDBsum5c0q
PubMed26187666
UniProtQ9AG27

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