Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1TAH

THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004806	molecular_function	triglyceride lipase activity
A	0005515	molecular_function	protein binding
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
B	0004806	molecular_function	triglyceride lipase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
C	0004806	molecular_function	triglyceride lipase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0016042	biological_process	lipid catabolic process
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0004806	molecular_function	triglyceride lipase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0016042	biological_process	lipid catabolic process
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 320

Chain	Residue
B	ASP241
B	ASP287
B	GLN291
B	VAL295

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 320

Chain	Residue
A	ASP241
A	ASP287
A	GLN291
A	VAL295

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 320

Chain	Residue
C	ASP241
C	ASP287
C	GLN291
C	VAL295

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA D 320

Chain	Residue
D	ASP241
D	ASP287
D	GLN291
D	VAL295

site_id	ACA
Number of Residues	4
Details	ACTIVE SITE

Chain	Residue
A	HIS285
A	ASP263
A	GLU288
A	SER87

site_id	ACB
Number of Residues	4
Details	ACTIVE SITE

Chain	Residue
B	SER87
B	HIS285
B	ASP263
B	GLU288

site_id	ACC
Number of Residues	4
Details	ACTIVE SITE

Chain	Residue
C	SER87
C	HIS285
C	ASP263
C	GLU288

site_id	ACD
Number of Residues	4
Details	ACTIVE SITE

Chain	Residue
D	SER87
D	HIS285
D	ASP263
D	GLU288

site_id	CAA
Number of Residues	4
Details	CALCIUM SITE NEAR TO THE ACTIVE SITE

Chain	Residue
A	ASP287
A	GLN291
A	ASP241
A	VAL295

site_id	CAB
Number of Residues	4
Details	CALCIUM SITE NEAR TO THE ACTIVE SITE

Chain	Residue
B	ASP287
B	GLN291
B	ASP241
B	VAL295

site_id	CAC
Number of Residues	4
Details	CALCIUM SITE NEAR TO THE ACTIVE SITE

Chain	Residue
C	ASP287
C	GLN291
C	ASP241
C	VAL295

site_id	CAD
Number of Residues	4
Details	CALCIUM SITE NEAR TO THE ACTIVE SITE

Chain	Residue
D	ASP287
D	GLN291
D	ASP241
D	VAL295

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	VAL81-GLY90

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000305\|PubMed:8683577

Chain	Residue	Details
B	ASN48
A	ASN48
C	ASN48
D	ASN48

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Charge relay system => ECO:0000305\|PubMed:8683577

Chain	Residue	Details
B	THR224
B	ALA246
A	THR224
A	ALA246
C	THR224
C	ALA246
D	THR224
D	ALA246

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P22088

Chain	Residue	Details
B	LEU49
C	GLN88
D	LEU17
D	GLN88
A	LEU49
C	LEU49
D	LEU49
B	LEU17
B	GLN88
A	LEU17
A	GLN88
C	LEU17

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:8683577, ECO:0007744\|PDB:1CVL, ECO:0007744\|PDB:1QGE

Chain	Residue	Details
B	SER202
C	LEU248
C	ALA252
C	ASN256
D	SER202
D	LEU248
D	ALA252
D	ASN256
B	LEU248
B	ALA252
B	ASN256
A	SER202
A	LEU248
A	ALA252
A	ASN256
C	SER202

site_id	SWS_FT_FI5
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:1476423, ECO:0000305\|PubMed:8405390

Chain	Residue	Details
B	SER87
A	SER87
C	SER87
D	SER87

site_id	SWS_FT_FI6
Number of Residues	8
Details	ACT_SITE: Charge relay system => ECO:0000269\|PubMed:1476423, ECO:0000305\|PubMed:8405390

Chain	Residue	Details
B	ASP263
B	HIS285
A	ASP263
A	HIS285
C	ASP263
C	HIS285
D	ASP263
D	HIS285

site_id	SWS_FT_FI7
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:16518399, ECO:0000269\|PubMed:8405390, ECO:0007744\|PDB:1TAH, ECO:0007744\|PDB:2ES4

Chain	Residue	Details
B	ASP241
C	ASP287
C	GLN291
C	VAL295
D	ASP241
D	ASP287
D	GLN291
D	VAL295
B	ASP287
B	GLN291
B	VAL295
A	ASP241
A	ASP287
A	GLN291
A	VAL295
C	ASP241

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details

Chain	Residue	Details
B	HIS285
B	SER87
B	ASP263

site_id	CSA2
Number of Residues	3
Details

Chain	Residue	Details
A	HIS285
A	SER87
A	ASP263

site_id	CSA3
Number of Residues	3
Details

Chain	Residue	Details
C	HIS285
C	SER87
C	ASP263

site_id	CSA4
Number of Residues	3
Details

Chain	Residue	Details
D	HIS285
D	SER87
D	ASP263

site_id	MCSA1
Number of Residues	9
Details	M-CSA 519

Chain	Residue	Details
B	LEU17	electrostatic stabiliser
B	SER87	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
B	GLN88	electrostatic stabiliser
B	ASP241	metal ligand
B	ASP263	electrostatic stabiliser, increase basicity, modifies pKa
B	HIS285	proton acceptor, proton donor
B	ASP287	metal ligand
B	GLN291	metal ligand
B	VAL295	metal ligand

site_id	MCSA2
Number of Residues	9
Details	M-CSA 519

Chain	Residue	Details
A	LEU17	electrostatic stabiliser
A	SER87	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLN88	electrostatic stabiliser
A	ASP241	metal ligand
A	ASP263	electrostatic stabiliser, increase basicity, modifies pKa
A	HIS285	proton acceptor, proton donor
A	ASP287	metal ligand
A	GLN291	metal ligand
A	VAL295	metal ligand

site_id	MCSA3
Number of Residues	9
Details	M-CSA 519

Chain	Residue	Details
C	LEU17	electrostatic stabiliser
C	SER87	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
C	GLN88	electrostatic stabiliser
C	ASP241	metal ligand
C	ASP263	electrostatic stabiliser, increase basicity, modifies pKa
C	HIS285	proton acceptor, proton donor
C	ASP287	metal ligand
C	GLN291	metal ligand
C	VAL295	metal ligand

site_id	MCSA4
Number of Residues	9
Details	M-CSA 519

Chain	Residue	Details
D	LEU17	electrostatic stabiliser
D	SER87	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
D	GLN88	electrostatic stabiliser
D	ASP241	metal ligand
D	ASP263	electrostatic stabiliser, increase basicity, modifies pKa
D	HIS285	proton acceptor, proton donor
D	ASP287	metal ligand
D	GLN291	metal ligand
D	VAL295	metal ligand

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)