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1V2G

The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004064molecular_functionarylesterase activity
A0004622molecular_functionlysophospholipase activity
A0006508biological_processproteolysis
A0006629biological_processlipid metabolic process
A0008233molecular_functionpeptidase activity
A0016297molecular_functionfatty acyl-[ACP] hydrolase activity
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0047617molecular_functionfatty acyl-CoA hydrolase activity
A0052816molecular_functionlong-chain fatty acyl-CoA hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AMET17
ASER18
AALA21
AILE42
AARG53
ALEU57
AARG160
AHOH621
AHOH633

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD A 601
ChainResidue
ALYS34
ATHR35
AGLN175
AVAL178

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OCA A 201
ChainResidue
AASP9
ASER10
AGLY44
AASN73
AARG108
APRO110
ATYR145
AHIS157

Functional Information from PROSITE/UniProt
site_idPS01098
Number of Residues11
DetailsLIPASE_GDSL_SER Lipolytic enzymes "G-D-S-L" family, serine active site. LLILGDSLs.AG
ChainResidueDetails
ALEU4-GLY14

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577, ECO:0000305|PubMed:8098033
ChainResidueDetails
ASER10

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577
ChainResidueDetails
AASP154
AHIS157

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15697222
ChainResidueDetails
AGLY44
AASN73

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bwp
ChainResidueDetails
AGLY44
ASER10
AASN73
AASP154
AHIS157

site_idMCSA1
Number of Residues5
DetailsM-CSA 755
ChainResidueDetails
ASER10covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY44electrostatic stabiliser
AASN73electrostatic stabiliser
AASP154electrostatic stabiliser, increase basicity
AHIS157electrostatic stabiliser, proton acceptor, proton donor

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PDB entries from 2025-06-11

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