1R1X
Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005829 | cellular_component | cytosol |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0015670 | biological_process | carbon dioxide transport |
| A | 0015671 | biological_process | oxygen transport |
| A | 0016020 | cellular_component | membrane |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0030185 | biological_process | nitric oxide transport |
| A | 0031720 | molecular_function | haptoglobin binding |
| A | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0043177 | molecular_function | organic acid binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071682 | cellular_component | endocytic vesicle lumen |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005829 | cellular_component | cytosol |
| B | 0005833 | cellular_component | hemoglobin complex |
| B | 0008217 | biological_process | regulation of blood pressure |
| 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 | 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 | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| B | 0042542 | biological_process | response to hydrogen peroxide |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0043177 | molecular_function | organic acid binding |
| B | 0045429 | biological_process | positive regulation of nitric oxide biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070293 | biological_process | renal absorption |
| B | 0070527 | biological_process | platelet aggregation |
| B | 0071682 | cellular_component | endocytic vesicle lumen |
| B | 0072562 | cellular_component | blood microparticle |
| B | 0097746 | biological_process | blood vessel diameter maintenance |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| B | 1904724 | cellular_component | tertiary granule lumen |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO A 142 |
| Chain | Residue |
| A | HIS58 |
| A | VAL62 |
| A | HEM143 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 143 |
| Chain | Residue |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| A | VAL93 |
| A | ASN97 |
| A | PHE98 |
| A | LEU101 |
| A | LEU136 |
| A | CMO142 |
| A | HOH252 |
| A | TYR42 |
| A | PHE43 |
| A | HIS45 |
| A | PHE46 |
| A | HIS58 |
| A | LYS61 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO B 147 |
| Chain | Residue |
| B | HIS63 |
| B | VAL67 |
| B | HEM148 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 148 |
| Chain | Residue |
| A | PRO4 |
| B | PHE41 |
| B | PHE42 |
| B | HIS63 |
| B | ALA70 |
| B | LEU88 |
| B | LEU91 |
| B | HIS92 |
| B | LEU96 |
| B | VAL98 |
| B | ASN102 |
| B | PHE103 |
| B | LEU106 |
| B | LEU141 |
| B | CMO147 |
| B | HOH225 |
| B | HOH241 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MBN A 201 |
| Chain | Residue |
| A | ALA13 |
| A | TRP14 |
| A | THR67 |
| A | VAL70 |
| A | LEU125 |
| A | MBN203 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MBN A 203 |
| Chain | Residue |
| A | ALA63 |
| A | LEU66 |
| A | LEU105 |
| A | LEU109 |
| A | MBN201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | HIS2 | |
| B | LEU3 | |
| B | GLY83 | |
| B | LYS144 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: distal binding residue |
| Chain | Residue | Details |
| B | GLY64 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: proximal binding residue |
| Chain | Residue | Details |
| B | CYS93 | |
| A | ARG92 | |
| A | VAL107 | |
| A | LEU109 | |
| A | HIS122 | |
| A | THR134 | |
| A | TRP14 | |
| A | GLY25 | |
| A | GLU30 | |
| A | PHE46 | |
| A | LEU48 | |
| A | ALA53 | |
| A | LYS56 | |
| A | LYS60 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 19 |
| Details | SITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 |
| Chain | Residue | Details |
| B | LYS8 | |
| B | LEU75 | |
| B | PHE85 | |
| B | CYS93 | |
| B | LEU105 | |
| B | VAL111 | |
| B | LYS120 | |
| B | THR123 | |
| B | ALA129 | |
| B | LEU141 | |
| B | TYR145 | |
| B | GLU26 | |
| B | ARG30 | |
| B | PRO36 | |
| B | THR38 | |
| B | GLY46 | |
| B | ALA53 | |
| B | ASN57 | |
| B | SER72 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Not glycated => ECO:0000269|PubMed:7358733 |
| Chain | Residue | Details |
| B | VAL60 | |
| B | GLY83 | |
| B | LEU96 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N-pyruvate 2-iminyl-valine; in Hb A1b |
| Chain | Residue | Details |
| B | HIS2 | |
| A | VAL17 | |
| A | THR41 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | ALA10 | |
| B | PHE45 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | ALA13 | |
| B | PRO51 | |
| B | LEU88 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:4531009 |
| Chain | Residue | Details |
| B | VAL60 | |
| B | GLY83 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411 |
| Chain | Residue | Details |
| B | ASP94 | |
| A | LEU125 | |
| A | VAL132 | |
| A | LYS139 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009 |
| Chain | Residue | Details |
| B | TYR145 | |
| A | VAL135 | |
| A | SER138 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569 |
| Chain | Residue | Details |
| B | HIS2 | |
| A | VAL17 | |
| A | THR41 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 |
| Chain | Residue | Details |
| B | SER9 | |
| B | VAL18 | |
| B | VAL67 | |
| B | GLU121 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 |
| Chain | Residue | Details |
| B | TYR145 |
