7DIF
GH127 beta-L-arabinofuranosidase HypBA1 covalently complexed with beta-L-arabinofuranose-configured cyclophellitol at 1.75-angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0102478 | molecular_function | beta-L-arabinofuranosidase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"24680821","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2014","firstPage":"1000171","lastPage":"1000171","volume":"4","journal":"J. Bioprocess. Biotech.","title":"Structure and catalytic mechanism of a glycoside hydrolase family-127 beta-L-arabinofuranosidase (HypBA1).","authors":["Huang C.H.","Zhu Z.","Cheng Y.S.","Chan H.C.","Ko T.P.","Chen C.C.","Wang I.","Ho M.R.","Hsu S.T.","Zeng Y.F.","Huang Y.N.","Liu J.R.","Guo R.T."],"citationCrossReferences":[{"database":"DOI","id":"10.4172/2155-9821.1000171"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; S-glycosyl-cysteine intermediate","evidences":[{"source":"PubMed","id":"24680821","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2014","firstPage":"1000171","lastPage":"1000171","volume":"4","journal":"J. Bioprocess. Biotech.","title":"Structure and catalytic mechanism of a glycoside hydrolase family-127 beta-L-arabinofuranosidase (HypBA1).","authors":["Huang C.H.","Zhu Z.","Cheng Y.S.","Chan H.C.","Ko T.P.","Chen C.C.","Wang I.","Ho M.R.","Hsu S.T.","Zeng Y.F.","Huang Y.N.","Liu J.R.","Guo R.T."],"citationCrossReferences":[{"database":"DOI","id":"10.4172/2155-9821.1000171"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24680821","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2014","firstPage":"1000171","lastPage":"1000171","volume":"4","journal":"J. Bioprocess. Biotech.","title":"Structure and catalytic mechanism of a glycoside hydrolase family-127 beta-L-arabinofuranosidase (HypBA1).","authors":["Huang C.H.","Zhu Z.","Cheng Y.S.","Chan H.C.","Ko T.P.","Chen C.C.","Wang I.","Ho M.R.","Hsu S.T.","Zeng Y.F.","Huang Y.N.","Liu J.R.","Guo R.T."],"citationCrossReferences":[{"database":"DOI","id":"10.4172/2155-9821.1000171"}]}},{"source":"PDB","id":"3WKX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WRG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24680821","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2014","firstPage":"1000171","lastPage":"1000171","volume":"4","journal":"J. Bioprocess. Biotech.","title":"Structure and catalytic mechanism of a glycoside hydrolase family-127 beta-L-arabinofuranosidase (HypBA1).","authors":["Huang C.H.","Zhu Z.","Cheng Y.S.","Chan H.C.","Ko T.P.","Chen C.C.","Wang I.","Ho M.R.","Hsu S.T.","Zeng Y.F.","Huang Y.N.","Liu J.R.","Guo R.T."],"citationCrossReferences":[{"database":"DOI","id":"10.4172/2155-9821.1000171"}]}},{"source":"PDB","id":"3WKX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WRE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WRG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
