1HQD

PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 613

Chain	Residue
A	ASP242
A	ASP288
A	GLN292
A	LEU293
A	VAL296
A	HOH326
A	HOH409

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE INK A 612

Chain	Residue
A	TYR29
A	SER87
A	GLN88
A	PHE119
A	LEU167
A	HIS286
A	GLY16
A	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
A	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
A	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
A	ASP264
A	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
A	LEU17
A	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
A	ASP242
A	ASP288
A	GLN292
A	VAL296

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1tah

Chain	Residue	Details
A	ASP264
A	HIS286
A	SER87

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site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1tah

Chain	Residue	Details
A	ASP264
A	HIS286
A	LEU17
A	GLN88
A	SER87

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