1L7A
structural Genomics, crystal structure of Cephalosporin C deacetylase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005976 | biological_process | polysaccharide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0030245 | biological_process | cellulose catabolic process |
| A | 0046555 | molecular_function | acetylxylan esterase activity |
| A | 0047739 | molecular_function | cephalosporin-C deacetylase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005976 | biological_process | polysaccharide metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0030245 | biological_process | cellulose catabolic process |
| B | 0046555 | molecular_function | acetylxylan esterase activity |
| B | 0047739 | molecular_function | cephalosporin-C deacetylase activity |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1odt |
| Chain | Residue | Details |
| A | SER181 | |
| A | ASP269 | |
| A | HIS298 | |
| A | GLN182 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1odt |
| Chain | Residue | Details |
| B | SER181 | |
| B | ASP269 | |
| B | HIS298 | |
| B | GLN182 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1odt |
| Chain | Residue | Details |
| A | SER181 | |
| A | HIS298 | |
| A | ASP269 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1odt |
| Chain | Residue | Details |
| B | SER181 | |
| B | HIS298 | |
| B | ASP269 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1odt |
| Chain | Residue | Details |
| A | HIS298 | |
| A | ASP269 | |
| A | ALA134 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 866 |
| Chain | Residue | Details |
| A | TYR91 | electrostatic stabiliser |
| A | SER181 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLN182 | electrostatic stabiliser |
| A | ASP269 | electrostatic stabiliser, increase basicity |
| A | HIS298 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 866 |
| Chain | Residue | Details |
| B | TYR91 | electrostatic stabiliser |
| B | SER181 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLN182 | electrostatic stabiliser |
| B | ASP269 | electrostatic stabiliser, increase basicity |
| B | HIS298 | proton acceptor, proton donor |
