3O19
Structure-function analysis of human L-Prostaglandin D Synthase bound with fatty acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001516 | biological_process | prostaglandin biosynthetic process |
| A | 0004667 | molecular_function | prostaglandin-D synthase activity |
| A | 0005501 | molecular_function | retinoid binding |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0010467 | biological_process | gene expression |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019371 | biological_process | cyclooxygenase pathway |
| A | 0031965 | cellular_component | nuclear membrane |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0043303 | biological_process | mast cell degranulation |
| A | 0045187 | biological_process | regulation of circadian sleep/wake cycle, sleep |
| A | 0046457 | biological_process | prostanoid biosynthetic process |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0051384 | biological_process | response to glucocorticoid |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OLA A 200 |
| Chain | Residue |
| A | LEU27 |
| A | THR119 |
| A | TYR121 |
| A | PLM201 |
| A | LYS31 |
| A | LEU34 |
| A | SER53 |
| A | PHE55 |
| A | ARG64 |
| A | MET66 |
| A | TYR79 |
| A | MET117 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLM A 201 |
| Chain | Residue |
| A | ASN23 |
| A | SER24 |
| A | TRP26 |
| A | LEU51 |
| A | MET66 |
| A | TYR79 |
| A | TYR88 |
| A | SER105 |
| A | PRO111 |
| A | ASP114 |
| A | ASP114 |
| A | PHE115 |
| A | MET117 |
| A | TYR121 |
| A | OLA200 |
| A | HOH287 |
| A | HOH341 |
Functional Information from PROSITE/UniProt
| site_id | PS00213 |
| Number of Residues | 14 |
| Details | LIPOCALIN Lipocalin signature. NFQqdKFLGRWFSA |
| Chain | Residue | Details |
| A | ASN5-ALA18 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20667974","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"23234360","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8336134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8336134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
