4QUV
Structure of an integral membrane delta(14)-sterol reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016126 | biological_process | sterol biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| A | 0050613 | molecular_function | Delta14-sterol reductase activity |
| A | 0050661 | molecular_function | NADP binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006694 | biological_process | steroid biosynthetic process |
| B | 0006696 | biological_process | ergosterol biosynthetic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016126 | biological_process | sterol biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| B | 0050613 | molecular_function | Delta14-sterol reductase activity |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NDP A 501 |
| Chain | Residue |
| A | THR254 |
| A | ASN359 |
| A | TYR360 |
| A | ASP399 |
| A | CYS403 |
| A | LYS406 |
| A | TYR407 |
| A | TYR414 |
| A | ASN316 |
| A | LYS319 |
| A | ARG323 |
| A | LEU345 |
| A | LEU346 |
| A | LEU347 |
| A | TRP352 |
| A | HIS357 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NDP B 501 |
| Chain | Residue |
| B | LYS319 |
| B | ARG323 |
| B | LEU345 |
| B | LEU346 |
| B | LEU347 |
| B | TRP352 |
| B | HIS357 |
| B | ASN359 |
| B | TYR360 |
| B | ASP399 |
| B | CYS403 |
| B | LYS406 |
| B | TYR407 |
| B | TYR414 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 380 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"25307054","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 80 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"25307054","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 204 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25307054","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25307054","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4QUV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
