1YS1

Burkholderia cepacia lipase complexed with hexylphosphonic acid (R)-2-methyl-3-phenylpropyl ester

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0004806	molecular_function	triglyceride lipase activity
X	0005576	cellular_component	extracellular region
X	0016042	biological_process	lipid catabolic process
X	0016787	molecular_function	hydrolase activity
X	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA X 400

Chain	Residue
X	ASP242
X	ASP288
X	GLN292
X	LEU293
X	VAL296
X	HOH702
X	HOH711

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 2HR X 600

Chain	Residue
X	SER87
X	GLN88
X	SER117
X	HIS286
X	LEU287
X	GLY16
X	LEU17

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
X	VAL81-GLY90

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:15850979, ECO:0000305|PubMed:18386861, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP

Chain	Residue	Details
X	SER87

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP

Chain	Residue	Details
X	ASP264
X	HIS286

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP

Chain	Residue	Details
X	LEU17
X	GLN88

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP

Chain	Residue	Details
X	GLN292
X	VAL296
X	ASP242
X	ASP288

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