Structure of PDB 2wnw Chain B

Receptor sequence

>2wnwB (length=445) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2)

MKGRLISSDPYRQQFLVERAVSFSHRQRDCSELISVLPRHALQQIDGFGG
SFTEGAGVVFNSMSEKTKAQFLSLYFSAQEHNYTLARMPIQSCDFSLGNY
AYVDSSADLQQGRLSFSRDEAHLIPLISGALRLNPHMKLMASPWSPPAFM
KTNNDMNGGGKLRRECYADWADIIINYLLEYRRHGINVQALSVQNEPVAV
KTWDSCLYSVEEETAFAVQYLRPRLARQGMDEMEIYIWDHDKDGLVDWAE
LAFADEANYKGINGLAFHWYTGDHFSQIQYLAQCLPDKKLLFSEGCVPME
SDAGSQIRHWHTYLHDMIGNFKSGCSGFIDWNLLLNSEGGPNHQGNLCEA
PIQYDAQNDVLRRNHSWYGIGHFCRYVRPGARVMLSSSYDNLLEEVGFVN
PDGERVLVVYNRDVQERRCRVLDGDKEIALTLPPSGASTLLWRQE

3D structure

• PDB: 2wnw Crystal Structure of the Salmonella Enterica Serovar Typhimurium Virulence Factor Srfj, a Glycoside Hydrolase Family Enzyme.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E196 E294 C296 N320
• Catalytic site (residue number reindexed from 1): E196 E294 C296 N320
• Enzyme Commision number: 3.2.1.75: glucan endo-1,6-beta-glucosidase.

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	GOL	B	S387 S388 E395	S387 S388 E395
BS02	GOL	B	D94 W144 E196 E294 W331	D94 W144 E196 E294 W331
BS03	GOL	B	P223 R224 R227	P223 R224 R227

Gene Ontology

Molecular Function

• GO:0004348 glucosylceramidase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0046557 glucan endo-1,6-beta-glucosidase activity

Biological Process

• GO:0006665 sphingolipid metabolic process
• GO:0006680 glucosylceramide catabolic process

External links

• PDB: RCSB:2wnw, PDBe:2wnw, PDBj:2wnw
• PDBsum: 2wnw
• PubMed: 19717598
• UniProt: Q9KIJ7