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4GI1

Structure of the complex of three phase partition treated lipase from Thermomyces lanuginosa with 16-hydroxypalmitic acid at 2.4 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriglyceride lipase activity
B0006629biological_processlipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AARG84
ASER85
AILE86
AGLU87
AGLY266
ATHR267

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 16Y A 302
ChainResidue
AARG81
ASER83
AARG84
ATRP89
AASN92
AASN94
AHIS110
ALEU147
ALEU151
AASP62
AVAL63
ATHR64

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BARG84
BSER85
BILE86
BGLU87
BTHR267

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 16Y B 302
ChainResidue
BASP62
BVAL63
BTHR64
BARG81
BSER83
BARG84
BTRP89
BASN92
BLEU93
BASN94
BHIS110
BLEU147
BLEU151

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VVFTGHSLGG
ChainResidueDetails
AVAL140-GLY149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:8014587
ChainResidueDetails
ASER146
BSER146

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:8014587
ChainResidueDetails
AASP201
AHIS258
BASP201
BHIS258

224931

PDB entries from 2024-09-11

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