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	ACT_SITE: Nucleophile; for thioesterase activity => ECO:0000250|UniProtKB:Q9ZGI2, ECO:0000305|PubMed:11752428, ECO:0000305|PubMed:26592346

Chain	Residue	Details
A	SER142

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor; for thioesterase activity => ECO:0000250|UniProtKB:Q9ZGI2, ECO:0000305|PubMed:11752428, ECO:0000305|PubMed:26592346

Chain	Residue	Details
A	HIS259

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9ZGI2

Chain	Residue	Details
A	THR76

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:26592346

Chain	Residue	Details
A	ALA143
A	ASP169

---

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

---