Structure of PDB 5ngl Chain C

Receptor sequence
>5nglC (length=452) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
GDVAIYTTTSSLTRDLTRDAVNFSTTITLNPAEQYQTMDGFGAAITGSTC
YNLLLMKPADRHAFLTETFSDKDGFGFSYIRISIGCSDFSLSEYTCCDTK
GIENFALQSEEKDYILPILKEILAINPSIKVIAAPWTCPKWMKVKSLTDR
TPLDSWTNGQLNPDYYQDYATYFVKWIQAFKAEGIDIYAVTPQNEPLNRG
NSASLYMEWEEQRDFVKTALGPQMKAAGLSTKIYAFDHNYNYDNIESQKN
YPGKIYEDAAASQYLAGAAYHNYGGNREELLNIHQAYPEKELLFTETSIG
TWNSGRDLSKRLMEDMEEVALGTINNWCKGVIVWNLMLDNDRGPNREGGC
QTCYGAVDINNSDYKTIIRNSHYYIIAHLSSVVKPGAVRIATTGYTDNGI
TCSAFENTDGTYAFVLINNNEKSKKITVSDGQRHFAYDVPGKSVTSYRWA
KS
3D structure
PDB5ngl A Bacteroidetes locus dedicated to fungal 1,6-beta-glucan degradation: Unique substrate conformation drives specificity of the key endo-1,6-beta-glucanase.
ChainC
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E238 E339 S341 D358
Catalytic site (residue number reindexed from 1) E195 E296 S298 D315
Enzyme Commision number ?
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 NOJ C D131 N237 E238 N244 Y316 E339 W377 D88 N194 E195 N201 Y273 E296 W334
BS02 BGC C W345 C393 W302 C350
Gene Ontology
Molecular Function
GO:0004348 glucosylceramidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0006665 sphingolipid metabolic process
GO:0006680 glucosylceramide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5ngl, PDBe:5ngl, PDBj:5ngl
PDBsum5ngl
PubMed28461332
UniProtQ8A2J3

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