3PE6
Crystal Structure of a soluble form of human MGLL in complex with an inhibitor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004622 | molecular_function | lysophospholipase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0006639 | biological_process | acylglycerol metabolic process |
A | 0006954 | biological_process | inflammatory response |
A | 0009966 | biological_process | regulation of signal transduction |
A | 0016020 | cellular_component | membrane |
A | 0016042 | biological_process | lipid catabolic process |
A | 0019369 | biological_process | arachidonic acid metabolic process |
A | 0019433 | biological_process | triglyceride catabolic process |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046464 | biological_process | acylglycerol catabolic process |
A | 0047372 | molecular_function | acylglycerol lipase activity |
A | 0050727 | biological_process | regulation of inflammatory response |
A | 0051930 | biological_process | regulation of sensory perception of pain |
A | 0052651 | biological_process | monoacylglycerol catabolic process |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
A | 2000124 | biological_process | regulation of endocannabinoid signaling pathway |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ZYH A 304 |
Chain | Residue |
A | GLY50 |
A | LEU241 |
A | VAL270 |
A | HOH365 |
A | HOH406 |
A | HOH441 |
A | ALA51 |
A | GLU53 |
A | HIS121 |
A | SER122 |
A | MET123 |
A | SER181 |
A | LEU184 |
A | TYR194 |
Functional Information from PROSITE/UniProt
site_id | PS00120 |
Number of Residues | 10 |
Details | LIPASE_SER Lipases, serine active site. VFLLGHSMGG |
Chain | Residue | Details |
A | VAL116-GLY125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:19957260 |
Chain | Residue | Details |
A | PRO112 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:19957260 |
Chain | Residue | Details |
A | VAL229 | |
A | LYS259 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O35678 |
Chain | Residue | Details |
A | THR10 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:O35678 |
Chain | Residue | Details |
A | SER48 |