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3HJU

Crystal structure of human monoglyceride lipase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004622molecular_functionphosphatidylcholine lysophospholipase activity
A0005515molecular_functionprotein binding
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006954biological_processinflammatory response
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0019369biological_processarachidonate metabolic process
A0019433biological_processtriglyceride catabolic process
A0042803molecular_functionprotein homodimerization activity
A0046464biological_processacylglycerol catabolic process
A0047372molecular_functionmonoacylglycerol lipase activity
A0050727biological_processregulation of inflammatory response
A0051930biological_processregulation of sensory perception of pain
A0052651biological_processmonoacylglycerol catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
A2000124biological_processregulation of endocannabinoid signaling pathway
B0004622molecular_functionphosphatidylcholine lysophospholipase activity
B0005515molecular_functionprotein binding
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006954biological_processinflammatory response
B0009966biological_processregulation of signal transduction
B0016020cellular_componentmembrane
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0019369biological_processarachidonate metabolic process
B0019433biological_processtriglyceride catabolic process
B0042803molecular_functionprotein homodimerization activity
B0046464biological_processacylglycerol catabolic process
B0047372molecular_functionmonoacylglycerol lipase activity
B0050727biological_processregulation of inflammatory response
B0051930biological_processregulation of sensory perception of pain
B0052651biological_processmonoacylglycerol catabolic process
B0052689molecular_functioncarboxylic ester hydrolase activity
B2000124biological_processregulation of endocannabinoid signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 417
ChainResidue
AALA51
AGLU53
AARG57
AHIS121
ATYR194
AVAL270

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 410
ChainResidue
BHIS121
BVAL270
BGLY50
BALA51
BGLU53

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VFLLGHSMGG
ChainResidueDetails
AVAL116-GLY125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19957260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"19957260","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O35678","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"O35678","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
AHIS269
ASER122
AASP239

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
BHIS269
BSER122
BASP239

245663

PDB entries from 2025-12-03

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