2JKA
Native structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron
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 | 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 | 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 | 6 |
Details | BINDING SITE FOR RESIDUE CA A1727 |
Chain | Residue |
A | GLU194 |
A | GLU508 |
A | GLU526 |
A | GLU532 |
A | EDO1728 |
A | HOH2682 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B1727 |
Chain | Residue |
B | GLU532 |
B | EDO1728 |
B | HOH2666 |
B | GLU194 |
B | GLU508 |
B | GLU526 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A1728 |
Chain | Residue |
A | GLU194 |
A | GLU508 |
A | GLU532 |
A | CA1727 |
A | HOH2682 |
A | HOH2874 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B1728 |
Chain | Residue |
B | GLU194 |
B | GLU508 |
B | GLU532 |
B | CA1727 |
B | HOH2666 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B1729 |
Chain | Residue |
B | TRP341 |
B | GLU391 |
B | TRP397 |
B | HIS437 |
B | GLU439 |
B | LYS467 |
B | HOH2866 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B1730 |
Chain | Residue |
B | PRO112 |
B | VAL113 |
B | TRP114 |
B | CYS516 |
B | PRO520 |
B | HOH2130 |
B | HOH2867 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B1731 |
Chain | Residue |
B | ASP333 |
B | LYS338 |
B | ASN372 |
B | TYR376 |
B | ILE603 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A1729 |
Chain | Residue |
A | GLU391 |
A | TRP397 |
A | TRP400 |
A | HIS437 |
A | GLU439 |
A | HOH2875 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A1730 |
Chain | Residue |
A | PRO112 |
A | VAL113 |
A | TRP114 |
A | CYS516 |
A | PRO520 |
A | HOH2126 |
A | HOH2876 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A1731 |
Chain | Residue |
A | ASP333 |
A | LYS338 |
A | ASN372 |
A | 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 |