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6MLK

Structure of Thioesterase from DEBS with a thioesterase-specific antibody

Functional Information from GO Data
ChainGOidnamespacecontents
A0009058biological_processbiosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL H 301
ChainResidue
HTYR107
HTYR108
LSER77

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
HTYR203-HIS209
LTYR213-HIS219

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9ZGI2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26592346","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 602
ChainResidueDetails
ASER142covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AALA143electrostatic stabiliser
AASP169electrostatic stabiliser, modifies pKa
AHIS259proton acceptor, proton donor

238582

PDB entries from 2025-07-09

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