1UMK
The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005741 | cellular_component | mitochondrial outer membrane |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005811 | cellular_component | lipid droplet |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006695 | biological_process | cholesterol biosynthetic process |
| A | 0006809 | biological_process | nitric oxide biosynthetic process |
| A | 0008015 | biological_process | blood circulation |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016126 | biological_process | sterol biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031966 | cellular_component | mitochondrial membrane |
| A | 0035578 | cellular_component | azurophil granule lumen |
| A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| A | 0071949 | molecular_function | FAD binding |
| A | 1903958 | cellular_component | nitric-oxide synthase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 1301 |
| Chain | Residue |
| A | ARG91 |
| A | PHE120 |
| A | GLY123 |
| A | GLY124 |
| A | LYS125 |
| A | MET126 |
| A | SER127 |
| A | THR181 |
| A | THR184 |
| A | HOH1419 |
| A | HOH1422 |
| A | PRO92 |
| A | HOH1438 |
| A | HOH1520 |
| A | HOH1708 |
| A | HOH1709 |
| A | HOH1710 |
| A | HOH1711 |
| A | HOH1790 |
| A | HOH1804 |
| A | HOH1805 |
| A | HOH2023 |
| A | TYR93 |
| A | THR94 |
| A | VAL108 |
| A | ILE109 |
| A | LYS110 |
| A | TYR112 |
| A | PHE113 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 112 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00716","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15502298","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1UMK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCN2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| A | TYR93 |
