4GLB

Structure of p-nitrobenzaldehyde inhibited lipase from Thermomyces lanuginosa at 2.69 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004806	molecular_function	triacylglycerol lipase activity
A	0006629	biological_process	lipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
B	0004806	molecular_function	triacylglycerol lipase activity
B	0006629	biological_process	lipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE XXH A 301

Chain	Residue
A	GLY61
A	SER83
A	ARG84
A	TRP89
A	LEU147

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	ASN11
A	PRO229
A	VAL230
A	PHE262

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE XXH B 301

Chain	Residue
B	SER83
B	ARG84
B	TRP89
B	LEU147
B	HOH415

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 302

Chain	Residue
B	SER58
B	GLY59

---

Functional Information from PROSITE/UniProt

site_id	PS00120
Number of Residues	10
Details	LIPASE_SER Lipases, serine active site. VVFTGHSLGG

Chain	Residue	Details
A	VAL140-GLY149

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"8014587","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"8014587","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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