3DHT
The Crystal Structure Determination of Rat (rattus norvegicus) Hemoglobin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001540 | molecular_function | amyloid-beta binding |
| A | 0001701 | biological_process | in utero embryonic development |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0009617 | biological_process | response to bacterium |
| 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 | 0030185 | biological_process | nitric oxide transport |
| A | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| A | 0035634 | biological_process | response to stilbenoid |
| A | 0045776 | biological_process | negative regulation of blood pressure |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048821 | biological_process | erythrocyte development |
| 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 | 0006749 | biological_process | glutathione metabolic process |
| B | 0006954 | biological_process | inflammatory response |
| 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 | 0030185 | biological_process | nitric oxide transport |
| 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 | 0042542 | biological_process | response to hydrogen peroxide |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048821 | biological_process | erythrocyte development |
| B | 0070293 | biological_process | renal absorption |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM A 142 |
| Chain | Residue |
| A | TYR42 |
| A | PHE98 |
| A | LEU101 |
| A | HOH149 |
| A | HIS45 |
| A | HIS58 |
| A | LYS61 |
| A | ALA65 |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| A | VAL93 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 147 |
| Chain | Residue |
| B | TYR41 |
| B | PHE42 |
| B | PHE45 |
| B | HIS63 |
| B | LYS66 |
| B | VAL67 |
| B | HIS92 |
| B | VAL98 |
| B | ASN102 |
| B | LEU106 |
| B | LEU141 |
| B | HOH149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Peptide: {"description":"Hemopressin","featureId":"PRO_0000455938","evidences":[{"source":"PubMed","id":"12500972","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"distal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"proximal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylvaline","evidences":[{"source":"UniProtKB","id":"P02086","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P02088","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Asymmetric dimethylarginine","evidences":[{"source":"UniProtKB","id":"P02089","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P11517","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
