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4GLB

Structure of p-nitrobenzaldehyde inhibited lipase from Thermomyces lanuginosa at 2.69 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriacylglycerol lipase activity
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriacylglycerol lipase activity
B0006629biological_processlipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE XXH A 301
ChainResidue
AGLY61
ASER83
AARG84
ATRP89
ALEU147

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AASN11
APRO229
AVAL230
APHE262

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE XXH B 301
ChainResidue
BSER83
BARG84
BTRP89
BLEU147
BHOH415

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BSER58
BGLY59

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

226707

PDB entries from 2024-10-30

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