4ATF

Crystal structure of inactivated mutant beta-agarase B in complex with agaro-octaose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0009279	cellular_component	cell outer membrane
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0033916	molecular_function	beta-agarase activity
A	0042803	molecular_function	protein homodimerization activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0009279	cellular_component	cell outer membrane
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0033916	molecular_function	beta-agarase activity
B	0042803	molecular_function	protein homodimerization activity
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
C	0009279	cellular_component	cell outer membrane
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0033916	molecular_function	beta-agarase activity
C	0042803	molecular_function	protein homodimerization activity
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process
D	0009279	cellular_component	cell outer membrane
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0033916	molecular_function	beta-agarase activity
D	0042803	molecular_function	protein homodimerization activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"G0L322","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"G0L322","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22778272","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	885
Details	Domain: {"description":"GH16","evidences":[{"source":"PROSITE-ProRule","id":"PRU01098","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---