Structure of PDB 4pys Chain A

Receptor sequence
>4pysA (length=492) Species: 272559 (Bacteroides fragilis NCTC 9343) [Search protein sequence]
GQIIMPTPGKIERADGRLRLQGKIRMYAEESPGSFIRLFYEKLVPESAVE
WCKEEVNSHISWKKDVTLPTEGYRIRVTPERIIVEAADDAGFIYAIQSLR
QWNTGEERGLIFPCVEITDFPRVKWRSFMLDSGRQYQKVSTIKKYIDMAS
MLKMNYFHWHLTEGLGWRIEIKRYPFLTRIGAFVGQGPEQQGFYSQEEVK
EIIGYAADRGITVVPEIDMPGHAEAALNAYPRLGCFNVAVKVPQNIFCAG
KDSTLIFLKNVLDEVCRMFPSAYIHLGGDPKGNWDKCPDCRSRIEKEKLK
DSHDLQLWFSARMADYLKQKGRKAIFWGDVIYKDGYSLPDNVVIQWWNWR
GHRDLALKNAVRHNYPVICGTNYYTYLNFPLTPWKGYTQARTFDLEDVYL
RNPSYRPREENPLILGMSSALWTDDGVTESMIDRRVFPRILALAEQMWHS
GNPENFDEFYGKVLSKQLWFEQQGYSFGPALKEDAGTNYKWD
3D structure
PDB4pys The crystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343
ChainA
Resolution1.822 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D303
Catalytic site (residue number reindexed from 1) D279
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 C272 C313 C316 C248 C287 C290
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030203 glycosaminoglycan metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:4pys, PDBe:4pys, PDBj:4pys
PDBsum4pys
PubMed
UniProtD1JST6

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