3CU9
High resolution crystal structure of 1,5-alpha-L-arabinanase from Geobacillus Stearothermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031222 | biological_process | arabinan catabolic process |
| A | 0046558 | molecular_function | arabinan endo-1,5-alpha-L-arabinosidase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 400 |
| Chain | Residue |
| A | HIS271 |
| A | HOH1001 |
| A | HOH1011 |
| A | HOH1018 |
| A | HOH1022 |
| A | HOH1028 |
| A | HOH1258 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GOL A 450 |
| Chain | Residue |
| A | TRP84 |
| A | PHE104 |
| A | ILE146 |
| A | ASP147 |
| A | GLU201 |
| A | CYS221 |
| A | TYR229 |
| A | HIS271 |
| A | HOH1003 |
| A | HOH1079 |
| A | HOH1083 |
| A | HOH1110 |
| A | HIS26 |
| A | ASP27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate","evidences":[{"source":"PubMed","id":"19505290","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for substrate recognition","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
