Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004974 | molecular_function | leukotriene receptor activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022900 | biological_process | electron transport chain |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue KNZ A 2001 |
| Chain | Residue |
| A | LYS37 |
| A | LEU198 |
| A | MET201 |
| A | GLY209 |
| A | ARG267 |
| A | LEU271 |
| A | HIS284 |
| A | HOH2108 |
| A | HOH2111 |
| A | HOH2112 |
| A | HOH2113 |
| A | TYR119 |
| A | TYR127 |
| A | ILE166 |
| A | SER169 |
| A | SER170 |
| A | LEU188 |
| A | LEU190 |
| A | LYS194 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue OLC A 2002 |
| Chain | Residue |
| A | SER83 |
| A | SER89 |
| A | PHE93 |
| A | PHE106 |
| A | GLU1081 |
| A | OLC2006 |
| A | OLA2013 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue OLC A 2003 |
| Chain | Residue |
| A | ARG38 |
| A | GLU39 |
| A | PRO42 |
| A | ILE43 |
| A | ILE47 |
| A | ARG282 |
| A | ALA286 |
| A | ILE289 |
| A | LEU293 |
| A | OLC2011 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue OLC A 2004 |
| Chain | Residue |
| A | LEU46 |
| A | PHE49 |
| A | PRO92 |
| A | ASP96 |
| A | LEU99 |
| A | ARG100 |
| A | THR265 |
| A | VAL269 |
| A | CYS279 |
| A | LEU283 |
| A | OLC2010 |
| A | OLA2012 |
| A | HOH2101 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 2005 |
| Chain | Residue |
| A | PHE36 |
| A | OLA2014 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 2006 |
| Chain | Residue |
| A | LEU86 |
| A | OLC2002 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue OLC A 2007 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 2009 |
| Chain | Residue |
| A | CYS299 |
| A | PHE300 |
| A | LEU303 |
| A | OLC2011 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 2010 |
| Chain | Residue |
| A | VAL53 |
| A | OLC2004 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue OLC A 2011 |
| Chain | Residue |
| A | LEU58 |
| A | SER59 |
| A | VAL62 |
| A | PHE63 |
| A | PRO302 |
| A | TYR305 |
| A | OLC2003 |
| A | OLC2009 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue OLA A 2012 |
| Chain | Residue |
| A | ASP96 |
| A | OLC2004 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 2013 |
| Chain | Residue |
| A | ILE105 |
| A | GLU1081 |
| A | OLC2002 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue OLA A 2014 |
| Chain | Residue |
| A | LYS285 |
| A | OLC2005 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 77 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
