2GDZ
Crystal structure of 15-hydroxyprostaglandin dehydrogenase type1, complexed with NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001822 | biological_process | kidney development |
| A | 0004957 | molecular_function | prostaglandin E receptor activity |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0007179 | biological_process | transforming growth factor beta receptor signaling pathway |
| A | 0007565 | biological_process | female pregnancy |
| A | 0007567 | biological_process | parturition |
| A | 0016323 | cellular_component | basolateral plasma membrane |
| A | 0016404 | molecular_function | 15-hydroxyprostaglandin dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019372 | biological_process | lipoxygenase pathway |
| A | 0030728 | biological_process | ovulation |
| A | 0032355 | biological_process | response to estradiol |
| A | 0032496 | biological_process | response to lipopolysaccharide |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043065 | biological_process | positive regulation of apoptotic process |
| A | 0045471 | biological_process | response to ethanol |
| A | 0045786 | biological_process | negative regulation of cell cycle |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0070493 | biological_process | thrombin-activated receptor signaling pathway |
| A | 0097070 | biological_process | ductus arteriosus closure |
| A | 1904707 | biological_process | positive regulation of vascular associated smooth muscle cell proliferation |
| A | 1905828 | biological_process | regulation of prostaglandin catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 300 |
| Chain | Residue |
| A | GLY12 |
| A | ASN91 |
| A | ALA92 |
| A | GLY93 |
| A | VAL94 |
| A | ILE106 |
| A | SER137 |
| A | SER138 |
| A | TYR151 |
| A | LYS155 |
| A | PRO183 |
| A | GLN15 |
| A | GLY184 |
| A | PHE185 |
| A | VAL186 |
| A | THR188 |
| A | ALA189 |
| A | ILE190 |
| A | HOH304 |
| A | HOH313 |
| A | HOH325 |
| A | HOH378 |
| A | GLY16 |
| A | HOH383 |
| A | HOH434 |
| A | HOH441 |
| A | ILE17 |
| A | ASP36 |
| A | TRP37 |
| A | CYS63 |
| A | ASP64 |
| A | VAL65 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlaglmpvaqQpvYCASKHGIvGFTrSAA |
| Chain | Residue | Details |
| A | SER138-ALA166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR151 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21072165 |
| Chain | Residue | Details |
| A | GLY12 | |
| A | ASP36 | |
| A | CYS63 | |
| A | ASN91 | |
| A | TYR151 | |
| A | VAL186 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | SER138 | |
| A | GLN148 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | LYS155 | |
| A | ASN107 | |
| A | SER138 | |
| A | TYR151 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | LYS155 | |
| A | GLN148 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | LYS155 | |
| A | TYR151 |
