2Y2W

Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046373	biological_process	L-arabinose metabolic process
A	0046556	molecular_function	alpha-L-arabinofuranosidase activity
B	0000272	biological_process	polysaccharide catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0046373	biological_process	L-arabinose metabolic process
B	0046556	molecular_function	alpha-L-arabinofuranosidase activity
C	0000272	biological_process	polysaccharide catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0046373	biological_process	L-arabinose metabolic process
C	0046556	molecular_function	alpha-L-arabinofuranosidase activity
D	0000272	biological_process	polysaccharide catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0046373	biological_process	L-arabinose metabolic process
D	0046556	molecular_function	alpha-L-arabinofuranosidase activity
E	0000272	biological_process	polysaccharide catabolic process
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0046373	biological_process	L-arabinose metabolic process
E	0046556	molecular_function	alpha-L-arabinofuranosidase activity
F	0000272	biological_process	polysaccharide catabolic process
F	0016787	molecular_function	hydrolase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0046373	biological_process	L-arabinose metabolic process
F	0046556	molecular_function	alpha-L-arabinofuranosidase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9XBQ3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q9XBQ3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9XBQ3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"Q9XBQ3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Site: {"description":"Important for substrate recognition","evidences":[{"source":"UniProtKB","id":"Q9XBQ3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---