3FOO
A Triangular Cytochrome b562 Superstructure Mediated by Ni Coordination - Monoclinic Form
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 |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0022900 | biological_process | electron transport chain |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0020037 | molecular_function | heme binding |
| F | 0022900 | biological_process | electron transport chain |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0020037 | molecular_function | heme binding |
| G | 0022900 | biological_process | electron transport chain |
| G | 0042597 | cellular_component | periplasmic space |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0005506 | molecular_function | iron ion binding |
| H | 0009055 | molecular_function | electron transfer activity |
| H | 0020037 | molecular_function | heme binding |
| H | 0022900 | biological_process | electron transport chain |
| H | 0042597 | cellular_component | periplasmic space |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0005506 | molecular_function | iron ion binding |
| I | 0009055 | molecular_function | electron transfer activity |
| I | 0020037 | molecular_function | heme binding |
| I | 0022900 | biological_process | electron transport chain |
| I | 0042597 | cellular_component | periplasmic space |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0005506 | molecular_function | iron ion binding |
| J | 0009055 | molecular_function | electron transfer activity |
| J | 0020037 | molecular_function | heme binding |
| J | 0022900 | biological_process | electron transport chain |
| J | 0042597 | cellular_component | periplasmic space |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0005506 | molecular_function | iron ion binding |
| K | 0009055 | molecular_function | electron transfer activity |
| K | 0020037 | molecular_function | heme binding |
| K | 0022900 | biological_process | electron transport chain |
| K | 0042597 | cellular_component | periplasmic space |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0005506 | molecular_function | iron ion binding |
| L | 0009055 | molecular_function | electron transfer activity |
| L | 0020037 | molecular_function | heme binding |
| L | 0022900 | biological_process | electron transport chain |
| L | 0042597 | cellular_component | periplasmic space |
| L | 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 | CYS98 |
| A | CYS101 |
| A | HIS102 |
| A | ARG106 |
| A | MET7 |
| A | LEU10 |
| A | ASN11 |
| A | MET33 |
| A | PRO45 |
| A | PHE61 |
| A | GLY64 |
| A | PHE65 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXX A 151 |
| Chain | Residue |
| A | GLN41 |
| A | LYS42 |
| A | ALA43 |
| A | PRO53 |
| A | MET58 |
| A | CYS59 |
| A | ALA62 |
| B | ASP73 |
| B | ASP74 |
| B | HIS77 |
| B | NI108 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI A 107 |
| Chain | Residue |
| A | ALA1 |
| A | ASP39 |
| A | HOH166 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI A 108 |
| Chain | Residue |
| A | HIS77 |
| C | HOH124 |
| C | HOH125 |
| C | PXX151 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 150 |
| Chain | Residue |
| B | GLU4 |
| B | MET7 |
| B | MET33 |
| B | PRO46 |
| B | PHE61 |
| B | PHE65 |
| B | THR97 |
| B | CYS98 |
| B | CYS101 |
| B | HIS102 |
| B | TYR105 |
| B | ARG106 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PXX B 151 |
| Chain | Residue |
| B | GLN41 |
| B | LYS42 |
| B | ALA43 |
| B | PRO53 |
| B | MET58 |
| B | CYS59 |
| B | ALA62 |
| C | ASP73 |
| C | ASP74 |
| C | HIS77 |
| C | NI108 |
| C | HOH123 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI B 107 |
| Chain | Residue |
| B | ALA1 |
| B | ASP39 |
| B | HOH171 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI B 108 |
| Chain | Residue |
| A | PXX151 |
| B | HIS77 |
| B | HOH121 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HEM C 150 |
| Chain | Residue |
| C | GLU4 |
| C | MET7 |
| C | PRO46 |
| C | PHE61 |
| C | PHE65 |
| C | THR97 |
| C | CYS98 |
| C | CYS101 |
| C | HIS102 |
| C | ARG106 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXX C 151 |
| Chain | Residue |
| A | ASP73 |
| A | ASP74 |
| A | HIS77 |
| A | NI108 |
| C | GLN41 |
| C | LYS42 |
| C | ALA43 |
| C | PRO53 |
| C | MET58 |
| C | CYS59 |
| C | ALA62 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI C 107 |
| Chain | Residue |
| C | ALA1 |
| C | ASP39 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI C 108 |
| Chain | Residue |
| B | HOH122 |
| B | PXX151 |
| C | HIS77 |
| C | HOH123 |
| site_id | BC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM D 150 |
| Chain | Residue |
| D | ARG106 |
| D | GLU4 |
| D | MET7 |
| D | ASN11 |
| D | PRO45 |
| D | PRO46 |
| D | PHE61 |
| D | PHE65 |
| D | CYS98 |
| D | CYS101 |
| D | HIS102 |
| D | TYR105 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXX D 151 |
| Chain | Residue |
| D | GLN41 |
| D | LYS42 |
| D | ALA43 |
| D | PRO53 |
| D | MET58 |
| D | CYS59 |
| D | ALA62 |
| E | ASP73 |
| E | ASP74 |
| E | HIS77 |
| E | NI108 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI D 107 |
| Chain | Residue |
| D | ALA1 |
| D | ASP39 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI D 108 |
| Chain | Residue |
| D | HIS77 |
| F | HOH118 |
| F | HOH119 |
| F | PXX151 |
| site_id | BC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM E 150 |
| Chain | Residue |
| E | LEU3 |
| E | GLU4 |
| E | MET7 |
| E | ASN11 |
| E | PHE61 |
| E | PHE65 |
| E | LEU68 |
| E | CYS98 |
| E | CYS101 |
| E | HIS102 |
| E | TYR105 |
| E | ARG106 |
| site_id | BC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXX E 151 |
| Chain | Residue |
| E | GLN41 |
| E | LYS42 |
| E | ALA43 |
| E | PRO53 |
| E | MET58 |
| E | CYS59 |
| E | ALA62 |
| F | ASP73 |
| F | ASP74 |
| F | HIS77 |
| F | NI108 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI E 107 |
| Chain | Residue |
| E | ALA1 |
| E | ASP39 |
| E | HOH149 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI E 108 |
| Chain | Residue |
| D | HOH113 |
| D | HOH114 |
| D | PXX151 |
| E | HIS77 |
| site_id | CC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEM F 150 |
| Chain | Residue |
| A | LYS85 |
| F | GLU4 |
| F | MET7 |
| F | PRO45 |
| F | PHE61 |
| F | PHE65 |
| F | CYS98 |
| F | CYS101 |
| F | HIS102 |
| F | TYR105 |
| F | ARG106 |
| site_id | CC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXX F 151 |
| Chain | Residue |
| D | ASP73 |
| D | ASP74 |
| D | HIS77 |
| D | NI108 |
| F | GLN41 |
| F | LYS42 |
| F | ALA43 |
| F | PRO53 |
| F | MET58 |
| F | CYS59 |
| F | ALA62 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI F 107 |
| Chain | Residue |
| F | ALA1 |
| F | ASP39 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI F 108 |
| Chain | Residue |
| E | HOH117 |
| E | PXX151 |
| F | HIS77 |
| F | HOH116 |
| site_id | CC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM G 150 |
| Chain | Residue |
| G | GLU4 |
| G | MET7 |
| G | ASN11 |
| G | LEU14 |
| G | PRO46 |
| G | PHE61 |
| G | PHE65 |
| G | CYS98 |
| G | CYS101 |
| G | HIS102 |
| G | TYR105 |
| G | ARG106 |
| site_id | CC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PXX G 151 |
| Chain | Residue |
| G | GLN41 |
| G | LYS42 |
| G | ALA43 |
| G | PRO53 |
| G | MET58 |
| G | CYS59 |
| H | ASP73 |
| H | ASP74 |
| H | HIS77 |
| H | NI108 |
| site_id | CC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI G 107 |
| Chain | Residue |
| G | ALA1 |
| G | ASP39 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI G 108 |
| Chain | Residue |
| G | HIS77 |
| G | HOH112 |
| I | HOH110 |
| I | PXX151 |
| site_id | DC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM H 150 |
| Chain | Residue |
| H | GLU4 |
| H | MET7 |
| H | ASN11 |
| H | LEU14 |
| H | PHE61 |
| H | PHE65 |
| H | THR97 |
| H | CYS98 |
| H | CYS101 |
| H | HIS102 |
| H | TYR105 |
| H | ARG106 |
| site_id | DC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXX H 151 |
| Chain | Residue |
| H | GLN41 |
| H | LYS42 |
| H | ALA43 |
| H | PRO53 |
| H | MET58 |
| H | CYS59 |
| H | ALA62 |
| I | ASP73 |
| I | ASP74 |
| I | HIS77 |
| I | NI108 |
| site_id | DC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI H 107 |
| Chain | Residue |
| H | ALA1 |
| H | ASP39 |
| site_id | DC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI H 108 |
| Chain | Residue |
| G | HOH109 |
| G | HOH110 |
| G | PXX151 |
| H | HIS77 |
| site_id | DC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM I 150 |
| Chain | Residue |
| I | GLU4 |
| I | MET7 |
| I | ASN11 |
| I | PRO45 |
| I | PRO46 |
| I | PHE61 |
| I | PHE65 |
| I | LEU68 |
| I | CYS98 |
| I | CYS101 |
| I | HIS102 |
| I | TYR105 |
| I | ARG106 |
| site_id | DC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PXX I 151 |
| Chain | Residue |
| G | ASP73 |
| G | ASP74 |
| G | HIS77 |
| G | NI108 |
| I | GLN41 |
| I | LYS42 |
| I | ALA43 |
| I | PRO53 |
| I | MET58 |
| I | CYS59 |
| site_id | DC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI I 107 |
| Chain | Residue |
| I | ALA1 |
| I | ASP39 |
| site_id | DC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI I 108 |
| Chain | Residue |
| H | HOH111 |
| H | HOH112 |
| H | PXX151 |
| I | HIS77 |
| site_id | EC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM J 150 |
| Chain | Residue |
| J | GLU4 |
| J | MET7 |
| J | ASN11 |
| J | PRO45 |
| J | PRO46 |
| J | PHE61 |
| J | PHE65 |
| J | CYS98 |
| J | CYS101 |
| J | HIS102 |
| J | TYR105 |
| J | ARG106 |
| site_id | EC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PXX J 151 |
| Chain | Residue |
| J | GLN41 |
| J | LYS42 |
| J | ALA43 |
| J | PRO53 |
| J | MET58 |
| J | CYS59 |
| J | ALA62 |
| L | ASP73 |
| L | ASP74 |
| L | HIS77 |
| L | NI108 |
| site_id | EC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI J 107 |
| Chain | Residue |
| J | ALA1 |
| J | ASP39 |
| J | HOH182 |
| site_id | EC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI J 108 |
| Chain | Residue |
| J | HIS77 |
| K | HOH112 |
| K | HOH113 |
| K | PXX151 |
| site_id | EC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM K 150 |
| Chain | Residue |
| K | GLU4 |
| K | MET7 |
| K | ASN11 |
| K | MET33 |
| K | PRO46 |
| K | PHE61 |
| K | PHE65 |
| K | CYS98 |
| K | CYS101 |
| K | HIS102 |
| K | TYR105 |
| K | ARG106 |
| site_id | EC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PXX K 151 |
| Chain | Residue |
| J | ASP74 |
| J | HIS77 |
| J | NI108 |
| K | GLN41 |
| K | LYS42 |
| K | ALA43 |
| K | PRO53 |
| K | MET58 |
| K | CYS59 |
| K | HOH112 |
| site_id | EC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI K 107 |
| Chain | Residue |
| K | ALA1 |
| K | ASP39 |
| site_id | EC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI K 108 |
| Chain | Residue |
| K | HIS77 |
| K | HOH128 |
| K | HOH129 |
| L | PXX151 |
| site_id | EC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEM L 150 |
| Chain | Residue |
| L | GLU4 |
| L | MET7 |
| L | PRO45 |
| L | PRO46 |
| L | PHE61 |
| L | PHE65 |
| L | THR97 |
| L | CYS98 |
| L | CYS101 |
| L | HIS102 |
| L | ARG106 |
| site_id | FC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PXX L 151 |
| Chain | Residue |
| K | ASP73 |
| K | ASP74 |
| K | HIS77 |
| K | NI108 |
| L | GLN41 |
| L | LYS42 |
| L | ALA43 |
| L | PRO53 |
| L | MET58 |
| L | CYS59 |
| site_id | FC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI L 107 |
| Chain | Residue |
| L | ALA1 |
| L | ASP39 |
| L | HOH194 |
| site_id | FC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI L 108 |
| Chain | Residue |
| J | HOH126 |
| J | PXX151 |
| L | HIS77 |
| L | HOH127 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 264 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 156 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
