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 | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005783 | cellular_component | endoplasmic reticulum |
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 | 0016020 | cellular_component | membrane |
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 | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0051384 | biological_process | response to glucocorticoid |
A | 0070062 | cellular_component | extracellular exosome |
A | 2000255 | biological_process | negative regulation of male germ cell proliferation |
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 | ACT_SITE: Nucleophile => ECO:0000269|PubMed:20667974 |
Chain | Residue | Details |
A | ALA37 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:23234360 |
Chain | Residue | Details |
A | SER1 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:8336134 |
Chain | Residue | Details |
A | ASN23 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8336134 |
Chain | Residue | Details |
A | ASN50 |