3C7E
Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from Bacillus subtilis.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0045493 | biological_process | xylan catabolic process |
| A | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 488 |
| Chain | Residue |
| A | GLU359 |
| A | GLU361 |
| A | ASN383 |
| A | GLN384 |
| A | ASP480 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 489 |
| Chain | Residue |
| A | HOH2361 |
| A | ARG368 |
| A | SER388 |
| A | GLN390 |
| A | ASP393 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 490 |
| Chain | Residue |
| A | HIS290 |
| A | HOH2067 |
| A | HOH2068 |
| A | HOH2128 |
| A | HOH2171 |
| A | HOH2184 |
| A | HOH2358 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 2055 |
| Chain | Residue |
| A | ASP219 |
| A | PRO268 |
| A | PHE269 |
| A | HOH2335 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 2056 |
| Chain | Residue |
| A | GLY32 |
| A | PHE296 |
| A | LYS297 |
| A | HOH2262 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 2057 |
| Chain | Residue |
| A | ASN342 |
| A | TYR343 |
| A | ALA344 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 2058 |
| Chain | Residue |
| A | ASP24 |
| A | LEU59 |
| A | ARG321 |
| A | HOH2322 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 129 |
| Details | Domain: {"description":"CBM6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00523","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18980579","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18980579","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18980579","evidenceCode":"ECO:0000269"}]} |
| 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":"18980579","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
