5ZUN
Crystal structure of human monoacylglycerol lipase in complex with compound 3l
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004622 | molecular_function | phosphatidylcholine lysophospholipase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0019369 | biological_process | arachidonate 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 | monoacylglycerol 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 | 24 |
| Details | binding site for residue 9JX A 401 |
| Chain | Residue |
| A | GLY50 |
| A | PRO178 |
| A | ILE179 |
| A | SER181 |
| A | LEU184 |
| A | SER185 |
| A | GLU190 |
| A | VAL191 |
| A | TYR194 |
| A | LEU205 |
| A | LEU241 |
| A | ALA51 |
| A | VAL270 |
| A | LYS273 |
| A | PG4402 |
| A | HOH542 |
| A | HOH585 |
| A | GLU53 |
| A | ARG57 |
| A | MET88 |
| A | HIS121 |
| A | SER122 |
| A | MET123 |
| A | GLY177 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PG4 A 402 |
| Chain | Residue |
| A | THR158 |
| A | 9JX401 |
| A | EDO403 |
| A | HOH501 |
| A | HOH519 |
| A | HOH532 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ILE179 |
| A | ASP180 |
| A | PG4402 |
| A | HOH522 |
| A | HOH673 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | GLU190 |
| A | HIS272 |
| A | LYS273 |
| A | PHE283 |
| A | HOH546 |
| A | HOH658 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | GLN12 |
| A | GLY81 |
| A | ARG87 |
| A | LEU199 |
| A | HOH565 |
| A | HOH621 |
| A | HOH677 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ILE14 |
| A | HOH563 |
| A | HOH589 |
| A | HOH597 |
| A | HOH632 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | TYR34 |
| A | HIS103 |
| A | SER106 |
| A | MET107 |
| A | SER196 |
| A | ARG202 |
| A | HOH508 |
| A | HOH574 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | HIS54 |
| A | GLY56 |
| A | ARG57 |
| A | ILE193 |
| A | ASP197 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | ARG9 |
| A | THR10 |
| A | PRO11 |
| A | GLU84 |
| A | GLY85 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | ASN215 |
| A | ARG219 |
| A | ARG222 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 411 |
| Chain | Residue |
| A | HIS94 |
| A | ARG219 |
| A | HOH791 |
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 | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19957260","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"19957260","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O35678","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"O35678","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
