Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| 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 |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0022900 | biological_process | electron transport chain |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0022900 | biological_process | electron transport chain |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0022900 | biological_process | electron transport chain |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM A 150 |
| Chain | Residue |
| A | GLU4 |
| A | HIS102 |
| A | ARG106 |
| C | ASN99 |
| C | GLN103 |
| A | MET7 |
| A | ASN11 |
| A | PRO45 |
| A | PRO46 |
| A | PHE61 |
| A | PHE65 |
| A | CYS98 |
| A | CYS101 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 151 |
| Chain | Residue |
| A | PRO53 |
| A | ASP54 |
| A | HIS59 |
| A | ARG62 |
| A | HIS63 |
| A | CYS67 |
| A | ZN109 |
| A | HOH112 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM B 150 |
| Chain | Residue |
| B | LEU3 |
| B | GLU4 |
| B | MET7 |
| B | ASN11 |
| B | PRO45 |
| B | PRO46 |
| B | PHE61 |
| B | PHE65 |
| B | CYS98 |
| B | CYS101 |
| B | HIS102 |
| B | ARG106 |
| B | HOH130 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 151 |
| Chain | Residue |
| B | CYS67 |
| B | ZN110 |
| B | HOH121 |
| C | PRO53 |
| C | HIS59 |
| C | ARG62 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM C 150 |
| Chain | Residue |
| C | MET7 |
| C | ASN11 |
| C | LEU14 |
| C | PRO45 |
| C | PRO46 |
| C | PHE61 |
| C | PHE65 |
| C | CYS98 |
| C | CYS101 |
| C | HIS102 |
| C | ARG106 |
| C | HOH110 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT C 151 |
| Chain | Residue |
| C | HIS63 |
| C | TRP66 |
| C | CYS67 |
| D | PRO53 |
| D | ASP54 |
| D | HIS59 |
| D | ARG62 |
| D | ZN107 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEM D 150 |
| Chain | Residue |
| D | GLU4 |
| D | MET7 |
| D | ASN11 |
| D | LEU14 |
| D | PRO45 |
| D | PHE61 |
| D | PHE65 |
| D | CYS98 |
| D | CYS101 |
| D | HIS102 |
| D | ARG106 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT D 151 |
| Chain | Residue |
| B | PRO53 |
| B | ASP54 |
| B | HIS59 |
| B | ARG62 |
| B | ZN109 |
| D | HIS63 |
| D | CYS67 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 107 |
| Chain | Residue |
| A | ALA1 |
| A | ASP39 |
| A | HIS77 |
| A | HOH111 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 108 |
| Chain | Residue |
| A | GLU8 |
| A | ASP12 |
| C | GLU8 |
| C | ASP12 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 109 |
| Chain | Residue |
| A | HIS59 |
| A | HIS63 |
| A | HOH112 |
| A | ACT151 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 107 |
| Chain | Residue |
| B | ALA1 |
| B | ASP39 |
| B | HOH120 |
| D | HIS77 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 108 |
| Chain | Residue |
| B | GLU8 |
| B | ASP12 |
| D | GLU8 |
| D | ASP12 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 109 |
| Chain | Residue |
| B | HIS59 |
| B | HOH112 |
| D | HIS63 |
| D | ACT151 |
| B | ASP54 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 110 |
| Chain | Residue |
| B | ACT151 |
| C | HIS59 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 111 |
| Chain | Residue |
| B | HIS77 |
| C | ALA1 |
| C | ASP39 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 107 |
| Chain | Residue |
| C | HIS63 |
| C | ACT151 |
| D | ASP54 |
| D | HIS59 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 108 |
| Chain | Residue |
| C | HIS77 |
| D | ALA1 |
| D | ASP39 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 110 |
| Chain | Residue |
| A | GLU57 |
| A | GLU57 |
| A | HOH131 |
| A | HOH131 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN D 109 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 88 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 52 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"axial binding residue"} |
