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3PE6

Crystal Structure of a soluble form of human MGLL in complex with an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004622molecular_functionlysophospholipase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006639biological_processacylglycerol metabolic process
A0006954biological_processinflammatory response
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0019369biological_processarachidonic acid metabolic process
A0019433biological_processtriglyceride catabolic process
A0042803molecular_functionprotein homodimerization activity
A0046464biological_processacylglycerol catabolic process
A0047372molecular_functionacylglycerol 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
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ZYH A 304
ChainResidue
AGLY50
ALEU241
AVAL270
AHOH365
AHOH406
AHOH441
AALA51
AGLU53
AHIS121
ASER122
AMET123
ASER181
ALEU184
ATYR194

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 Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:19957260
ChainResidueDetails
APRO112

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:19957260
ChainResidueDetails
AVAL229
ALYS259

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O35678
ChainResidueDetails
ATHR10

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:O35678
ChainResidueDetails
ASER48

218853

PDB entries from 2024-04-24

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