1T1N
CRYSTAL STRUCTURE OF CARBONMONOXY HEMOGLOBIN
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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE HEM A 143 |
Chain | Residue |
A | LYS62 |
A | GLN87 |
A | HIS88 |
A | LEU92 |
A | ASN98 |
A | LEU102 |
A | LEU137 |
A | CMO144 |
A | TYR42 |
A | PHE43 |
A | HIS45 |
A | TRP46 |
A | HIS59 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CMO A 144 |
Chain | Residue |
A | HIS59 |
A | VAL63 |
A | HEM143 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM B 147 |
Chain | Residue |
B | TYR41 |
B | PHE42 |
B | HIS63 |
B | LYS66 |
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 | STA |
Number of Residues | 2 |
Details | HEME GROUPS ARE BOUND TO CO |
Chain | Residue |
A | HIS88 |
A | HEM143 |
site_id | STB |
Number of Residues | 2 |
Details | HEME GROUPS ARE BOUND TO CO |
Chain | Residue |
B | HIS92 |
B | HEM147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: distal binding residue => ECO:0000269|PubMed:12093902, ECO:0007744|PDB:1LA6 |
Chain | Residue | Details |
B | HIS63 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: proximal binding residue => ECO:0000269|PubMed:12093902, ECO:0007744|PDB:1LA6, ECO:0007744|PDB:1T1N, ECO:0007744|PDB:3D1K, ECO:0007744|PDB:3NFE, ECO:0007744|PDB:3NG6 |
Chain | Residue | Details |
B | HIS92 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:8144556 |
Chain | Residue | Details |
A | SER1 |