5ZLE
Human duodenal cytochrome b (Dcytb) in substrate free form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005765 | cellular_component | lysosomal membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0010039 | biological_process | response to iron ion |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| A | 0031526 | cellular_component | brush border membrane |
| A | 0033215 | biological_process | reductive iron assimilation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0060586 | biological_process | multicellular organismal-level iron ion homeostasis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0140571 | molecular_function | transmembrane ascorbate ferrireductase activity |
| A | 0140575 | molecular_function | transmembrane monodehydroascorbate reductase activity |
| A | 0140576 | biological_process | ascorbate homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue HEM A 401 |
| Chain | Residue |
| A | TRP30 |
| A | MET116 |
| A | SER118 |
| A | HIS120 |
| A | SER121 |
| A | VAL170 |
| A | THR173 |
| A | ALA174 |
| A | GLY177 |
| A | LEU178 |
| A | GLU180 |
| A | PHE47 |
| A | LYS181 |
| A | HIS50 |
| A | PRO51 |
| A | MET54 |
| A | VAL104 |
| A | PHE105 |
| A | HIS108 |
| A | ASN115 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue HEM A 402 |
| Chain | Residue |
| A | ILE66 |
| A | TYR69 |
| A | ARG70 |
| A | LYS79 |
| A | HIS86 |
| A | ASN90 |
| A | TYR131 |
| A | GLN134 |
| A | GLY138 |
| A | PHE139 |
| A | PHE142 |
| A | LEU143 |
| A | MET156 |
| A | HIS159 |
| A | VAL160 |
| A | LYS225 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 83 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:30272000 |
| Chain | Residue | Details |
| A | MET1-TRP7 | |
| A | ARG70-SER78 | |
| A | PRO145-LEU151 | |
| A | GLN223-MET286 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | ARG8-LEU32 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 43 |
| Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:30272000 |
| Chain | Residue | Details |
| A | HIS33-PHE47 | |
| A | GLU106-SER118 | |
| A | GLU180-GLU197 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | ASN48-TYR69 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | LYS79-PHE105 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 25 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | LEU119-LEU144 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 27 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | ARG152-THR179 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | GLY198-PRO222 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | HIS50 | |
| A | HIS86 | |
| A | HIS120 | |
| A | HIS159 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30272000, ECO:0007744|PDB:5ZLE, ECO:0007744|PDB:5ZLG |
| Chain | Residue | Details |
| A | ARG70 | |
| A | LYS79 | |
| A | LYS83 | |
| A | HIS108 | |
| A | ASN115 | |
| A | ARG152 | |
| A | GLU180 | |
| A | LYS225 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER232 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR285 |
