3D3I
Crystal structural of Escherichia coli K12 YgjK, a glucosidase belonging to glycoside hydrolase family 63
Replaces: 2DS3Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004555 | molecular_function | alpha,alpha-trehalase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005991 | biological_process | trehalose metabolic process |
| A | 0005993 | biological_process | trehalose catabolic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009313 | biological_process | oligosaccharide catabolic process |
| A | 0015926 | molecular_function | glucosidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1902687 | cellular_component | glucosidase complex |
| B | 0004555 | molecular_function | alpha,alpha-trehalase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005991 | biological_process | trehalose metabolic process |
| B | 0005993 | biological_process | trehalose catabolic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009313 | biological_process | oligosaccharide catabolic process |
| B | 0015926 | molecular_function | glucosidase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1902687 | cellular_component | glucosidase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1001 |
| Chain | Residue |
| A | ASP431 |
| A | ASN433 |
| A | ASN435 |
| A | GLU439 |
| A | GLU549 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1001 |
| Chain | Residue |
| B | GLU549 |
| B | ASP431 |
| B | ASN433 |
| B | ASN435 |
| B | GLU439 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 2001 |
| Chain | Residue |
| A | PRO308 |
| A | PHE315 |
| A | TRP321 |
| A | ASP324 |
| A | LYS391 |
| A | PHE742 |
| A | TRP744 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 2002 |
| Chain | Residue |
| A | TRP321 |
| A | ASP368 |
| A | LYS391 |
| A | TRP496 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 2001 |
| Chain | Residue |
| B | PRO308 |
| B | PHE315 |
| B | TRP321 |
| B | ASP324 |
| B | LYS391 |
| B | PHE742 |
| B | TRP744 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 2002 |
| Chain | Residue |
| B | TRP321 |
| B | ASP368 |
| B | LYS391 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP501 | |
| B | ASP501 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU727 | |
| B | GLU727 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP431 | |
| B | VAL437 | |
| B | GLU439 | |
| B | GLU549 | |
| A | ASN433 | |
| A | ASN435 | |
| A | VAL437 | |
| A | GLU439 | |
| A | GLU549 | |
| B | ASP431 | |
| B | ASN433 | |
| B | ASN435 |
