6MLK
Structure of Thioesterase from DEBS with a thioesterase-specific antibody
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue CL H 301 |
Chain | Residue |
H | TYR107 |
H | TYR108 |
L | SER77 |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH |
Chain | Residue | Details |
H | TYR203-HIS209 | |
L | TYR213-HIS219 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
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_FI2 |
Number of Residues | 1 |
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_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9ZGI2","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"26592346","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
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 |