1EX9

CRYSTAL STRUCTURE OF THE PSEUDOMONAS AERUGINOSA LIPASE COMPLEXED WITH RC-(RP,SP)-1,2-DIOCTYLCARBAMOYL-GLYCERO-3-O-OCTYLPHOSPHONATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004806	molecular_function	triglyceride lipase activity
A	0005576	cellular_component	extracellular region
A	0015628	biological_process	protein secretion by the type II secretion system
A	0016042	biological_process	lipid catabolic process
A	0016298	molecular_function	lipase activity
A	0016787	molecular_function	hydrolase activity
A	0043952	biological_process	protein transport by the Sec complex
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 286

Chain	Residue
A	ASP209
A	ASP253
A	GLN257
A	VAL258
A	LEU261
A	HOH470
A	HOH483

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OCP A 382

Chain	Residue
A	LEU17
A	TYR27
A	SER82
A	HIS83
A	SER112
A	LEU159
A	HIS251
A	VAL258
A	GLY15
A	MET16

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL76-GLY85

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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:10893416, ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9

Chain	Residue	Details
A	SER82

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000305|PubMed:10893416, ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9

Chain	Residue	Details
A	ASP229
A	HIS251

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:10893416, ECO:0007744|PDB:1EX9

Chain	Residue	Details
A	MET16
A	HIS83
A	ASP209
A	ASP253
A	GLN257
A	LEU261

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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	ASP229
A	HIS251
A	SER82

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