2JKP
Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004339 | molecular_function | glucan 1,4-alpha-glucosidase activity |
| A | 0004558 | molecular_function | alpha-1,4-glucosidase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005983 | biological_process | starch catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004339 | molecular_function | glucan 1,4-alpha-glucosidase activity |
| B | 0004558 | molecular_function | alpha-1,4-glucosidase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005983 | biological_process | starch catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CTS A1727 |
| Chain | Residue |
| A | TRP331 |
| A | VAL471 |
| A | HIS507 |
| A | GLU508 |
| A | GLU526 |
| A | GLU532 |
| A | CA1728 |
| A | HOH2434 |
| A | HOH2519 |
| A | HOH2527 |
| A | ILE335 |
| A | TRP341 |
| A | GLU391 |
| A | TRP397 |
| A | TRP400 |
| A | HIS437 |
| A | GLU439 |
| A | LYS467 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CTS B1727 |
| Chain | Residue |
| B | TRP331 |
| B | ILE335 |
| B | TRP341 |
| B | GLU391 |
| B | TRP397 |
| B | TRP400 |
| B | HIS437 |
| B | GLU439 |
| B | LYS467 |
| B | VAL471 |
| B | HIS507 |
| B | GLU508 |
| B | GLU526 |
| B | GLU532 |
| B | CA1728 |
| B | HOH2447 |
| B | HOH2598 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B1728 |
| Chain | Residue |
| B | GLU194 |
| B | GLU508 |
| B | GLU526 |
| B | GLU532 |
| B | CTS1727 |
| B | HOH2144 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A1728 |
| Chain | Residue |
| A | GLU194 |
| A | GLU508 |
| A | GLU526 |
| A | GLU532 |
| A | CTS1727 |
| A | HOH2527 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1729 |
| Chain | Residue |
| A | PRO112 |
| A | VAL113 |
| A | TRP114 |
| A | CYS516 |
| A | PRO520 |
| A | HOH2090 |
| A | HOH2656 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1730 |
| Chain | Residue |
| A | ASP333 |
| A | LYS338 |
| A | ASN372 |
| A | TYR376 |
| A | ILE603 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B1729 |
| Chain | Residue |
| B | PRO112 |
| B | VAL113 |
| B | TRP114 |
| B | CYS516 |
| B | PRO520 |
| B | HOH2064 |
| B | HOH2599 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1730 |
| Chain | Residue |
| B | ASP333 |
| B | LYS338 |
| B | ASN372 |
| B | TYR376 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:18981178 |
| Chain | Residue | Details |
| A | GLU532 | |
| B | GLU532 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18981178 |
| Chain | Residue | Details |
| A | GLU194 | |
| A | GLU508 | |
| A | GLU526 | |
| A | GLU532 | |
| B | GLU194 | |
| B | GLU508 | |
| B | GLU526 | |
| B | GLU532 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PRO215 | |
| A | HIS437 | |
| A | HIS507 | |
| B | PRO215 | |
| B | HIS437 | |
| B | HIS507 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | SITE: Substrate |
| Chain | Residue | Details |
| A | GLU194 | |
| A | TRP331 | |
| A | LYS467 | |
| B | GLU194 | |
| B | TRP331 | |
| B | LYS467 |
