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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 107 |
| Chain | Residue |
| A | ALA1 |
| A | ASP39 |
| A | HIS77 |
| A | HOH228 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 108 |
| Chain | Residue |
| A | GLU8 |
| A | ASP12 |
| C | GLU8 |
| C | ASP12 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 109 |
| Chain | Residue |
| A | HIS63 |
| A | ACT151 |
| A | HOH259 |
| A | HIS59 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 150 |
| Chain | Residue |
| A | GLU4 |
| A | MET7 |
| A | ASN11 |
| A | PRO45 |
| A | PRO46 |
| A | PHE61 |
| A | PHE65 |
| A | CYS98 |
| A | CYS101 |
| A | HIS102 |
| A | TYR105 |
| A | ARG106 |
| A | HOH221 |
| A | HOH224 |
| A | HOH229 |
| A | HOH292 |
| C | GLN103 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 151 |
| Chain | Residue |
| A | ASP54 |
| A | HIS59 |
| A | ARG62 |
| A | HIS63 |
| A | CYS67 |
| A | ZN109 |
| A | HOH283 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 107 |
| Chain | Residue |
| B | ALA1 |
| B | ASP39 |
| B | HOH220 |
| D | HIS77 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 108 |
| Chain | Residue |
| B | GLU8 |
| B | ASP12 |
| D | GLU8 |
| D | ASP12 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 109 |
| Chain | Residue |
| B | ASP54 |
| B | HIS59 |
| B | HOH247 |
| D | HIS63 |
| D | ACT107 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 110 |
| Chain | Residue |
| B | HIS63 |
| B | ACT151 |
| C | ASP54 |
| C | HIS59 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 111 |
| Chain | Residue |
| B | HIS77 |
| C | ALA1 |
| C | ASP39 |
| C | HOH209 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 150 |
| Chain | Residue |
| B | GLU4 |
| B | MET7 |
| B | PRO45 |
| B | PRO46 |
| B | PHE61 |
| B | PHE65 |
| B | CYS98 |
| B | CYS101 |
| B | HIS102 |
| B | TYR105 |
| B | ARG106 |
| B | HOH293 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 151 |
| Chain | Residue |
| B | HIS63 |
| B | CYS67 |
| B | ZN110 |
| B | HOH202 |
| C | PRO53 |
| C | ASP54 |
| C | HIS59 |
| C | ARG62 |
| site_id | BC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM C 150 |
| Chain | Residue |
| C | GLU4 |
| C | MET7 |
| C | ASN11 |
| C | PRO45 |
| C | PRO46 |
| C | PHE61 |
| C | PHE65 |
| C | CYS98 |
| C | CYS101 |
| C | HIS102 |
| C | ARG106 |
| C | ARG106 |
| C | HOH213 |
| C | HOH221 |
| C | HOH224 |
| C | HOH280 |
| C | HOH292 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT D 107 |
| Chain | Residue |
| D | HIS63 |
| D | CYS67 |
| B | PRO53 |
| B | ASP54 |
| B | HIS59 |
| B | ARG62 |
| B | ZN109 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 108 |
| Chain | Residue |
| C | HIS63 |
| D | ASP54 |
| D | HIS59 |
| D | ACT151 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 109 |
| Chain | Residue |
| C | HIS77 |
| D | ALA1 |
| D | ASP39 |
| D | HOH225 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT D 151 |
| Chain | Residue |
| C | HIS63 |
| C | CYS67 |
| D | PRO53 |
| D | ASP54 |
| D | HIS59 |
| D | ARG62 |
| D | ZN108 |
| site_id | BC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM D 150 |
| Chain | Residue |
| D | GLU4 |
| D | MET7 |
| D | PRO45 |
| D | PRO46 |
| D | PHE61 |
| D | PHE65 |
| D | CYS98 |
| D | CYS101 |
| D | HIS102 |
| D | TYR105 |
| D | ARG106 |
| D | HOH213 |
| D | HOH233 |
| D | HOH274 |
| D | HOH298 |
| site_id | CC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM E 150 |
| Chain | Residue |
| B | THR31 |
| B | ALA34 |
| B | ALA38 |
| B | TRP66 |
| B | HIS73 |
| B | ASN80 |
| C | ALA38 |
| C | ASP39 |
| C | TRP41 |
| E | THR97 |
| E | CYS98 |
| E | CYS101 |
| E | HIS102 |
| E | HOH202 |
| E | HOH204 |
| E | HOH205 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | MET7 | |
| A | HIS102 | |
| B | MET7 | |
| B | HIS102 | |
| C | MET7 | |
| C | HIS102 | |
| D | MET7 | |
| D | HIS102 | |
