1JEB
Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human Zeta2 / Mouse Beta2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0015670 | biological_process | carbon dioxide transport |
| A | 0015671 | biological_process | oxygen transport |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048821 | biological_process | erythrocyte development |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005833 | cellular_component | hemoglobin complex |
| B | 0010999 | biological_process | regulation of eIF2 alpha phosphorylation by heme |
| B | 0015670 | biological_process | carbon dioxide transport |
| B | 0015671 | biological_process | oxygen transport |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0030097 | biological_process | hemopoiesis |
| B | 0030492 | molecular_function | hemoglobin binding |
| B | 0031720 | molecular_function | haptoglobin binding |
| B | 0031721 | molecular_function | hemoglobin alpha binding |
| B | 0031722 | molecular_function | hemoglobin beta binding |
| B | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048821 | biological_process | erythrocyte development |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0005344 | molecular_function | oxygen carrier activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005833 | cellular_component | hemoglobin complex |
| C | 0015670 | biological_process | carbon dioxide transport |
| C | 0015671 | biological_process | oxygen transport |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048821 | biological_process | erythrocyte development |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0005344 | molecular_function | oxygen carrier activity |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005833 | cellular_component | hemoglobin complex |
| D | 0010999 | biological_process | regulation of eIF2 alpha phosphorylation by heme |
| D | 0015670 | biological_process | carbon dioxide transport |
| D | 0015671 | biological_process | oxygen transport |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0030097 | biological_process | hemopoiesis |
| D | 0030492 | molecular_function | hemoglobin binding |
| D | 0031720 | molecular_function | haptoglobin binding |
| D | 0031721 | molecular_function | hemoglobin alpha binding |
| D | 0031722 | molecular_function | hemoglobin beta binding |
| D | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| D | 0043209 | cellular_component | myelin sheath |
| D | 0044877 | molecular_function | protein-containing complex binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048821 | biological_process | erythrocyte development |
| D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 142 |
| Chain | Residue |
| A | TYR42 |
| A | LEU91 |
| A | VAL93 |
| A | ASN97 |
| A | PHE98 |
| A | LEU101 |
| A | LEU136 |
| A | CMO143 |
| A | PHE43 |
| A | HIS45 |
| A | PHE46 |
| A | HIS58 |
| A | LYS61 |
| A | ALA65 |
| A | LEU83 |
| A | HIS87 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO A 143 |
| Chain | Residue |
| A | HIS58 |
| A | VAL62 |
| A | HEM142 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM B 147 |
| Chain | Residue |
| B | THR38 |
| B | TYR41 |
| B | PHE45 |
| B | HIS63 |
| B | ALA70 |
| B | LEU88 |
| B | LEU91 |
| B | HIS92 |
| B | LEU96 |
| B | VAL98 |
| B | ASN102 |
| B | PHE103 |
| B | LEU106 |
| B | LEU141 |
| B | CMO148 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO B 148 |
| Chain | Residue |
| B | HIS63 |
| B | VAL67 |
| B | HEM147 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM C 142 |
| Chain | Residue |
| B | HIS77 |
| C | TYR42 |
| C | PHE43 |
| C | HIS45 |
| C | PHE46 |
| C | HIS58 |
| C | LYS61 |
| C | LEU86 |
| C | HIS87 |
| C | LEU91 |
| C | VAL93 |
| C | ASN97 |
| C | PHE98 |
| C | LEU101 |
| C | CMO143 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO C 143 |
| Chain | Residue |
| C | HIS58 |
| C | VAL62 |
| C | HEM142 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM D 147 |
| Chain | Residue |
| D | TYR41 |
| D | PHE42 |
| D | PHE45 |
| D | HIS63 |
| D | LYS66 |
| D | LEU88 |
| D | LEU91 |
| D | HIS92 |
| D | LEU96 |
| D | VAL98 |
| D | ASN102 |
| D | LEU106 |
| D | LEU141 |
| D | CMO148 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO D 148 |
| Chain | Residue |
| D | HIS63 |
| D | VAL67 |
| D | HEM147 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"distal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"11747442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6172357","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"distal binding residue","evidences":[{"source":"UniProtKB","id":"P80044","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"11747442","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JEB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HRW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylvaline","evidences":[{"source":"UniProtKB","id":"P02086","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02091","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Asymmetric dimethylarginine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P11517","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 144 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
