1F5O
2.9 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED LAMPREY HEMOGLOBIN V IN THE SPACE GROUP P2(1)2(1)2(1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0015671 | biological_process | oxygen transport |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0015671 | biological_process | oxygen transport |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005344 | molecular_function | oxygen carrier activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0015671 | biological_process | oxygen transport |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005344 | molecular_function | oxygen carrier activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0015671 | biological_process | oxygen transport |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005344 | molecular_function | oxygen carrier activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0015671 | biological_process | oxygen transport |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0019825 | molecular_function | oxygen binding |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005344 | molecular_function | oxygen carrier activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0015671 | biological_process | oxygen transport |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0019825 | molecular_function | oxygen binding |
| F | 0020037 | molecular_function | heme binding |
| F | 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 | PHE51 |
| A | PHE109 |
| A | VAL111 |
| A | TYR115 |
| A | LEU119 |
| A | PHE52 |
| A | LYS54 |
| A | HIS73 |
| A | ARG76 |
| A | ILE77 |
| A | ALA80 |
| A | LYS104 |
| A | HIS105 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM B 150 |
| Chain | Residue |
| B | PHE51 |
| B | PHE52 |
| B | LYS54 |
| B | HIS73 |
| B | ARG76 |
| B | ALA80 |
| B | LYS104 |
| B | HIS105 |
| B | PHE109 |
| B | VAL111 |
| B | TYR115 |
| B | PHE116 |
| B | LEU119 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM C 150 |
| Chain | Residue |
| C | PHE51 |
| C | PHE52 |
| C | LYS54 |
| C | HIS73 |
| C | ARG76 |
| C | ALA80 |
| C | LYS104 |
| C | HIS105 |
| C | PHE109 |
| C | VAL111 |
| C | PHE116 |
| C | LEU119 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM D 150 |
| Chain | Residue |
| D | PHE51 |
| D | PHE52 |
| D | LYS54 |
| D | HIS73 |
| D | ARG76 |
| D | ALA80 |
| D | LYS104 |
| D | HIS105 |
| D | PHE109 |
| D | VAL111 |
| D | TYR115 |
| D | PHE116 |
| D | LEU119 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM E 150 |
| Chain | Residue |
| E | PHE51 |
| E | PHE52 |
| E | LYS54 |
| E | HIS73 |
| E | ARG76 |
| E | ALA80 |
| E | LYS104 |
| E | HIS105 |
| E | PHE109 |
| E | VAL111 |
| E | LEU119 |
| E | LEU145 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM F 150 |
| Chain | Residue |
| F | PHE51 |
| F | PHE52 |
| F | LYS54 |
| F | HIS73 |
| F | ARG76 |
| F | ALA80 |
| F | LYS104 |
| F | HIS105 |
| F | PHE109 |
| F | VAL111 |
| F | TYR115 |
| F | PHE116 |
| F | LEU119 |
| F | LEU145 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 834 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"distal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4032476","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4032476","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
