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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 500 |
| Chain | Residue |
| B | ASP2 |
| B | ALA43 |
| B | THR44 |
| B | HOH529 |
| C | LYS42 |
| C | HOH526 |
| C | HOH537 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| C | GLN103 |
| B | ARG106 |
| B | HOH522 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 502 |
| Chain | Residue |
| D | GLY82 |
| D | VAL84 |
| D | LYS85 |
| D | HOH503 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | LYS83 |
| A | VAL84 |
| A | LYS85 |
| A | GLU86 |
| A | HOH531 |
| C | LYS85 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| B | LYS51 |
| B | SER55 |
| B | GLU57 |
| D | LYS51 |
| D | SER52 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 505 |
| Chain | Residue |
| B | HIS102 |
| B | ARG106 |
| C | GLN103 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 506 |
| Chain | Residue |
| A | ARG106 |
| A | HEC150 |
| C | LYS32 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 507 |
| Chain | Residue |
| A | THR96 |
| A | ASN99 |
| C | LYS19 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 508 |
| Chain | Residue |
| C | GLY82 |
| C | LYS83 |
| C | VAL84 |
| C | LYS85 |
| C | HOH530 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEC A 150 |
| Chain | Residue |
| A | GLU4 |
| A | MET7 |
| A | GLU8 |
| A | MET33 |
| A | PRO46 |
| A | PHE61 |
| A | PHE65 |
| A | CYS98 |
| A | CYS101 |
| A | HIS102 |
| A | TYR105 |
| A | ARG106 |
| C | SO4506 |
| D | GLU4 |
| D | HEC150 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC B 150 |
| Chain | Residue |
| B | GLU4 |
| B | MET7 |
| B | GLU8 |
| B | MET33 |
| B | PRO45 |
| B | PRO46 |
| B | PHE61 |
| B | PHE65 |
| B | CYS98 |
| B | CYS101 |
| B | HIS102 |
| B | TYR105 |
| B | ARG106 |
| D | GLU18 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HEC C 150 |
| Chain | Residue |
| C | GLU4 |
| C | MET7 |
| C | GLU8 |
| C | PHE61 |
| C | PHE65 |
| C | CYS98 |
| C | CYS101 |
| C | HIS102 |
| C | ARG106 |
| site_id | BC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEC D 150 |
| Chain | Residue |
| A | GLU4 |
| A | GLU49 |
| A | HEC150 |
| D | LEU3 |
| D | GLU4 |
| D | MET7 |
| D | GLU8 |
| D | ASN11 |
| D | PRO45 |
| D | PRO46 |
| D | PHE61 |
| D | PHE65 |
| D | CYS98 |
| D | CYS101 |
| D | HIS102 |
| D | ARG106 |
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"} |