3BOM
Crystal structure of trout hemoglobin at 1.35 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0015671 | biological_process | oxygen transport |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0031720 | molecular_function | haptoglobin binding |
| A | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0043177 | molecular_function | organic acid binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0072562 | cellular_component | blood microparticle |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005833 | cellular_component | hemoglobin complex |
| B | 0015671 | biological_process | oxygen transport |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0031720 | molecular_function | haptoglobin binding |
| B | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0043177 | molecular_function | organic acid binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0072562 | cellular_component | blood microparticle |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005344 | molecular_function | oxygen carrier activity |
| C | 0005833 | cellular_component | hemoglobin complex |
| C | 0015671 | biological_process | oxygen transport |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0031720 | molecular_function | haptoglobin binding |
| C | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| C | 0042744 | biological_process | hydrogen peroxide catabolic process |
| C | 0043177 | molecular_function | organic acid binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0072562 | cellular_component | blood microparticle |
| C | 0098869 | biological_process | cellular oxidant detoxification |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0005344 | molecular_function | oxygen carrier activity |
| D | 0005833 | cellular_component | hemoglobin complex |
| D | 0015671 | biological_process | oxygen transport |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0031720 | molecular_function | haptoglobin binding |
| D | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| D | 0042744 | biological_process | hydrogen peroxide catabolic process |
| D | 0043177 | molecular_function | organic acid binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0072562 | cellular_component | blood microparticle |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 143 |
| Chain | Residue |
| A | TYR42 |
| A | VAL94 |
| A | ASN98 |
| A | PHE99 |
| A | LEU102 |
| A | LEU137 |
| A | HOH225 |
| A | HOH246 |
| A | HOH251 |
| A | HOH263 |
| A | HOH318 |
| A | PHE43 |
| A | HOH319 |
| A | HOH321 |
| A | HOH343 |
| A | HOH345 |
| A | HIS45 |
| A | TRP46 |
| A | HIS59 |
| A | THR62 |
| A | LEU87 |
| A | HIS88 |
| A | LEU92 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM B 148 |
| Chain | Residue |
| B | HIS41 |
| B | PHE45 |
| B | HIS63 |
| B | VAL67 |
| B | MET91 |
| B | HIS92 |
| B | LEU96 |
| B | ASN102 |
| B | PHE103 |
| B | LEU106 |
| B | LEU142 |
| B | HOH2941 |
| B | HOH2958 |
| D | LYS95 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM C 143 |
| Chain | Residue |
| C | TYR42 |
| C | PHE43 |
| C | HIS45 |
| C | TRP46 |
| C | HIS59 |
| C | THR62 |
| C | HIS88 |
| C | LEU92 |
| C | VAL94 |
| C | ASN98 |
| C | LEU102 |
| C | LEU137 |
| C | EDO2775 |
| C | HOH2837 |
| C | HOH2889 |
| C | HOH2925 |
| C | HOH2942 |
| C | HOH2949 |
| C | HOH2951 |
| C | HOH2959 |
| C | HOH2980 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM D 148 |
| Chain | Residue |
| D | HIS63 |
| D | VAL67 |
| D | LEU88 |
| D | MET91 |
| D | HIS92 |
| D | LEU96 |
| D | ASN102 |
| D | PHE103 |
| D | LEU106 |
| D | LEU142 |
| D | HOH2903 |
| D | HOH2934 |
| D | HOH2957 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 2775 |
| Chain | Residue |
| A | HOH166 |
| B | ARG104 |
| B | ALA107 |
| B | ASP108 |
| B | GLN132 |
| B | HOH2836 |
| B | HOH2978 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 2775 |
| Chain | Residue |
| D | ARG104 |
| D | ALA107 |
| D | ASP108 |
| D | GLN132 |
| D | VAL139 |
| D | HOH2811 |
| D | HOH2918 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 2775 |
| Chain | Residue |
| C | TRP46 |
| C | LYS58 |
| C | HIS59 |
| C | THR62 |
| C | HEM143 |
| C | HOH2830 |
| C | HOH2964 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 2776 |
| Chain | Residue |
| C | GLU26 |
| C | SER30 |
| C | PRO51 |
| C | GLY52 |
| C | HOH2781 |
| C | HOH2953 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"2706274","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 290 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"distal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue"} |
| Chain | Residue | Details |






