4KRX
Structure of Aes from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008126 | molecular_function | acetylesterase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0034338 | molecular_function | short-chain carboxylesterase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008126 | molecular_function | acetylesterase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0034338 | molecular_function | short-chain carboxylesterase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008126 | molecular_function | acetylesterase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0034338 | molecular_function | short-chain carboxylesterase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PG4 A 401 |
| Chain | Residue |
| A | GLY93 |
| A | HOH698 |
| A | HOH702 |
| A | HOH737 |
| A | GLY94 |
| A | SER165 |
| A | ALA166 |
| A | LEU197 |
| A | LEU216 |
| A | TYR224 |
| A | HOH553 |
| A | HOH582 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PG4 B 401 |
| Chain | Residue |
| B | GLY93 |
| B | GLY94 |
| B | PHE95 |
| B | SER165 |
| B | LEU197 |
| B | LEU216 |
| B | TYR224 |
| B | HOH538 |
| B | HOH637 |
| B | HOH659 |
Functional Information from PROSITE/UniProt
| site_id | PS01173 |
| Number of Residues | 17 |
| Details | LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. LFyLHGGGFilgNldTH |
| Chain | Residue | Details |
| A | LEU87-HIS103 |
| site_id | PS01174 |
| Number of Residues | 13 |
| Details | LIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. IgFAGDSAGAmLA |
| Chain | Residue | Details |
| A | ILE159-ALA171 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Motif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
