1KEZ
Crystal Structure of the Macrocycle-forming Thioesterase Domain of Erythromycin Polyketide Synthase (DEBS TE)
Functional Information from GO Data
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 618 |
| Details | Region: {"description":"Thioesterase","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Nucleophile; for thioesterase activity","evidences":[{"source":"UniProtKB","id":"Q9ZGI2","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"11752428","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26592346","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor; for thioesterase activity","evidences":[{"source":"UniProtKB","id":"Q9ZGI2","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"11752428","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26592346","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9ZGI2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26592346","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11752428 |
| Chain | Residue | Details |
| A | SER142 | |
| A | HIS259 | |
| A | ALA143 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 602 |
| Chain | Residue | Details |
| A | SER142 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ALA143 | electrostatic stabiliser |
| A | ASP169 | electrostatic stabiliser, modifies pKa |
| A | HIS259 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 602 |
| Chain | Residue | Details |
| B | SER142 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ALA143 | electrostatic stabiliser |
| B | ASP169 | electrostatic stabiliser, modifies pKa |
| B | HIS259 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 602 |
| Chain | Residue | Details |
| C | SER142 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ALA143 | electrostatic stabiliser |
| C | ASP169 | electrostatic stabiliser, modifies pKa |
| C | HIS259 | proton acceptor, proton donor |
