4G5D
X-ray crystal structure of Prostaglandin f synthase from Leishmania major Friedlin bound to NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001516 | biological_process | prostaglandin biosynthetic process |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001516 | biological_process | prostaglandin biosynthetic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDP A 301 |
| Chain | Residue |
| A | GLY23 |
| A | GLN171 |
| A | TRP197 |
| A | SER198 |
| A | PRO199 |
| A | LEU200 |
| A | GLY201 |
| A | GLN202 |
| A | GLY203 |
| A | LEU206 |
| A | ILE238 |
| A | VAL24 |
| A | PRO239 |
| A | LYS240 |
| A | SER241 |
| A | VAL242 |
| A | HIS243 |
| A | ARG246 |
| A | GLU249 |
| A | ASN250 |
| A | HOH427 |
| A | HOH434 |
| A | TRP25 |
| A | HOH436 |
| A | HOH437 |
| A | HOH439 |
| A | HOH440 |
| A | HOH546 |
| A | HOH573 |
| A | ASP49 |
| A | TYR54 |
| A | HIS112 |
| A | TRP113 |
| A | SER149 |
| A | ASN150 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NDP B 301 |
| Chain | Residue |
| B | GLY23 |
| B | VAL24 |
| B | TRP25 |
| B | ASP49 |
| B | TYR54 |
| B | LYS79 |
| B | HIS112 |
| B | SER149 |
| B | ASN150 |
| B | GLN171 |
| B | TRP197 |
| B | SER198 |
| B | PRO199 |
| B | LEU200 |
| B | GLY201 |
| B | GLN202 |
| B | GLY203 |
| B | LEU206 |
| B | ALA223 |
| B | ILE238 |
| B | PRO239 |
| B | LYS240 |
| B | SER241 |
| B | VAL242 |
| B | HIS243 |
| B | ARG246 |
| B | GLU249 |
| B | ASN250 |
| B | HOH437 |
| B | HOH440 |
| B | HOH441 |
| B | HOH564 |
| B | HOH568 |
| B | HOH586 |
| B | HOH599 |
| B | HOH632 |
| B | HOH786 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. FeqlykekkVRAIGVSNF |
| Chain | Residue | Details |
| A | PHE134-PHE151 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVHreRIeENaDI |
| Chain | Residue | Details |
| A | ILE238-ILE253 |
| site_id | PS00798 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDTAaiyknEesVG |
| Chain | Residue | Details |
| A | GLY44-GLY61 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
