Structure of PDB 3wwg Chain B

Receptor sequence
>3wwgB (length=542) Species: 5061 (Aspergillus niger) [Search protein sequence]
FMAVTANNSQLLTWWHNTGEINTQTPVADGNVRQSGLYSVKVQTTPASSS
LYYDSFVYLAIPGNGMSDQLQYTQGYNQTQAWTSFLYSHDATVKISRNGS
ANSNVVIRPTSLNFPVRYDNQSVYITVPYSPTGYRFSVEFDDDLISLAPS
GARQPENALLIFASPFENSSTKPQPGSPNSIAPAPGRVLGLNTTSASTVV
FNPGVYYFTGHDHMVLSSSVTWVYFAPGAYVKGAVEFLSTASEVKASGHG
VLSGEQYVWYADPDEGYQKASANNNGLRMWRGTLGNSSQTFVLNGVTVSA
PPFNSMDWSGNSLDLITCRVDDYKQVGAFYGQTDGLEMYPGTILQDVFYH
TDDDGLKMYYSNVTARNIVMWKESVAPVVEFGWTPRNTENVLFDNVDVIH
QAYANAGNNPGIFGAVNNYLYAPSSAHSTGNSNMTVRNITWSNFRAEGSS
SALFRINPIQNLDNISIKNVSIESFEPLSINTTESWMPVWYDLNNGKQIT
VTDFSIEGFTVGNTTITASNAASVGRIDGVDPAYAGSVHYID
3D structure
PDB3wwg The side chain of a glycosylated asparagine residue is important for the stability of isopullulanase
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D353 D372
Catalytic site (residue number reindexed from 1) D334 D353
Enzyme Commision number 3.2.1.57: isopullulanase.
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 BGC B N323 Q351 D353 D372 D373 W402 N304 Q332 D334 D353 D354 W383
BS02 GLC B N293 Y438 N274 Y419
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0051675 isopullulanase activity
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:3wwg, PDBe:3wwg, PDBj:3wwg
PDBsum3wwg
PubMed25359784
UniProtO00105|IPUA_ASPNG Isopullulanase (Gene Name=ipuA)

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