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7L4T

Crystal structure of human monoacylglycerol lipase in complex with compound 1

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
A0006633biological_processfatty acid biosynthetic process
A0006639biological_processacylglycerol metabolic process
A0006954biological_processinflammatory response
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
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
B0004622molecular_functionlysophospholipase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006639biological_processacylglycerol metabolic process
B0006954biological_processinflammatory response
B0009966biological_processregulation of signal transduction
B0016020cellular_componentmembrane
B0016042biological_processlipid catabolic process
B0019369biological_processarachidonic acid metabolic process
B0019433biological_processtriglyceride catabolic process
B0042803molecular_functionprotein homodimerization activity
B0046464biological_processacylglycerol catabolic process
B0047372molecular_functionacylglycerol 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 Residues12
Detailsbinding site for residue XPD A 2501
ChainResidue
AALA51
ALEU214
AHIS269
AVAL270
AGLU53
AARG57
AHIS121
ASER122
AMET123
ALEU184
ATYR194
ALEU205

site_idAC2
Number of Residues1
Detailsbinding site for residue ACT A 2502
ChainResidue
ATYR111

site_idAC3
Number of Residues4
Detailsbinding site for residue MPD B 401
ChainResidue
BLEU241
BMPD402
BMPD403
BHOH528

site_idAC4
Number of Residues7
Detailsbinding site for residue MPD B 402
ChainResidue
BALA151
BASN152
BSER155
BLEU205
BGLY210
BMPD401
BHOH608

site_idAC5
Number of Residues9
Detailsbinding site for residue MPD B 403
ChainResidue
BGLY50
BALA51
BGLU53
BHIS121
BTYR194
BVAL270
BMPD401
BHOH541
BHOH565

site_idAC6
Number of Residues3
Detailsbinding site for residue MPD B 404
ChainResidue
AGLN102
BHOH503
BHOH530

site_idAC7
Number of Residues1
Detailsbinding site for residue ACT B 405
ChainResidue
BTYR111

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
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:19957260
ChainResidueDetails
ASER122
BSER122

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:19957260
ChainResidueDetails
AASP239
AHIS269
BASP239
BHIS269

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O35678
ChainResidueDetails
ATHR10
BTHR10

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:O35678
ChainResidueDetails
ATYR58
BTYR58

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PDB entries from 2024-07-10

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