Structure of PDB 5c0q Chain A

Receptor sequence
>5c0qA (length=450) Species: 2337 (Thermotoga neapolitana) [Search protein sequence]
DLGKLFFCGFDDFNEEAREVIQKYRPAGVLIYPGVLSKEYLFLDFMNFLS
RNGRFIVSSDHEGGQLEVLKYVPSFPGNLAAGKVDPVFTGRYCEMAGRIM
NTLGFNMVFAPVLDLLSELRSFGSDPEVVASHGMEACMGYFKGGVIPCIK
HFPGHGKTADDSHYLLPTVNASFEELWREDLLPFRRIFQSRVKTAVMTAH
VKYPAVDDLPATLSKKLITEVLREKLNFKGLVLSDAMEMKAISENFSVEE
AVRFFIEAGGNMILLDNFRDLPVYYESLKKLIEDGSIERGKVERSIKIVD
EYLSALENRFNSGLIAEVAERAIECTRMRKELLGREVVLLVPSNTTGDDY
DLIPEVAKRFFKVRDVIRYDIEAGPDDVDGELIFDFVVNASKNEQVLQAH
LSLPSDRTIYFIIRNPFDAKFFPGRSVVITHSTKPISVYKSFQHLLGRCS
3D structure
PDB5c0q Crystal structure of beta-N-acetylglucosaminidase CbsA from Thermotoga neapolitana
ChainA
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 A D117 H161 H165 D114 H151 H155
BS02 ZN A D171 H173 D161 H163
BS03 ZN A R54 E327 E330 R51 E317 E320
BS04 ZN A E346 E398 E336 E381
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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