1JRL

Crystal structure of E. coli Lysophospholiase L1/Acyl-CoA Thioesterase I/Protease I L109P mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004064	molecular_function	arylesterase activity
A	0004622	molecular_function	lysophospholipase activity
A	0006508	biological_process	proteolysis
A	0006629	biological_process	lipid metabolic process
A	0008233	molecular_function	peptidase activity
A	0016297	molecular_function	fatty acyl-[ACP] hydrolase activity
A	0016298	molecular_function	lipase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0042802	molecular_function	identical protein binding
A	0047617	molecular_function	fatty acyl-CoA hydrolase activity
A	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
A	0102545	molecular_function	phosphatidyl phospholipase B activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 501

Chain	Residue
A	MET17
A	SER18
A	ALA21
A	ILE42
A	ARG53
A	LEU57
A	ARG160
A	HOH1029
A	HOH1047

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IMD A 601

Chain	Residue
A	LYS34
A	THR35
A	VAL178
A	HOH1166

---

Functional Information from PROSITE/UniProt

site_id	PS01098
Number of Residues	11
Details	LIPASE_GDSL_SER Lipolytic enzymes "G-D-S-L" family, serine active site. LLILGDSLs.AG

Chain	Residue	Details
A	LEU4-GLY14

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577, ECO:0000305|PubMed:8098033

Chain	Residue	Details
A	SER10

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577

Chain	Residue	Details
A	ASP154
A	HIS157

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15697222

Chain	Residue	Details
A	ASN73
A	GLY44

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 755

Chain	Residue	Details
A	SER10	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLY44	electrostatic stabiliser
A	ASN73	electrostatic stabiliser
A	ASP154	electrostatic stabiliser, increase basicity
A	HIS157	electrostatic stabiliser, proton acceptor, proton donor

---