Structure of PDB 3n18 Chain A

Receptor sequence
>3n18A (length=327) Species: 1396 (Bacillus cereus) [Search protein sequence]
NLGSKLLVGYWHNFDNGTGIIKLKDVSPKWDVINVSFGETGGDRSTVEFS
PVYGTDADFKSDISYLKSKGKKVVLSIGGQNGVVLLPDNAAKDRFINSIQ
SLIDKYGFDGIDIDLGSGIYLNGNDTNFKNPTTPQIVNLISAIRTISDHY
GPDFLLSMAPETAYVQGGYSAYGSIWGAYLPIIYGVKDKLTYIHVQHFNA
GSGIGMDGNNYNQGTADYEVAMADMLLHGFPVGGNANNIFPALRSDQVMI
GLPAAPAAAPSGGYISPTEMKKALNYIIKGVPFGGKYKLSNQSGYPAFRG
LMSWSINWDAKNNFEFSNNYRTYFDGL
3D structure
PDB3n18 Crystal structures of bacillus cereus NCTU2 chitinase complexes with chitooligomers reveal novel substrate binding for catalysis: a chitinase without chitin-binding and insertion domains
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.14: chitinase.
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 NAG A G145 E190 N228 G116 E161 N199
BS02 NAG A Q109 E190 Q225 N228 Q80 E161 Q196 N199
BS03 NAG A Q109 D143 Q225 N228 A287 W333 Q80 D114 Q196 N199 A258 W304
BS04 NAG A N45 F66 Q109 P289 W333 N16 F37 Q80 P260 W304
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008061 chitin binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3n18, PDBe:3n18, PDBj:3n18
PDBsum3n18
PubMed20685646
UniProtD0VV09

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