1IWH
Crystal Structure of Horse Carbonmonoxyhemoglobin-Bezafibrate Complex at 1.55A Resolution: A Novel Allosteric Binding Site in R-State 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 | 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 | 0031721 | molecular_function | hemoglobin alpha 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 | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 142 |
| Chain | Residue |
| A | TYR42 |
| A | ASN97 |
| A | PHE98 |
| A | LEU101 |
| A | LEU136 |
| A | CMO143 |
| A | PEM501 |
| A | HOH1007 |
| A | HOH1070 |
| A | HOH1119 |
| A | HOH1126 |
| A | HIS58 |
| A | HOH1127 |
| A | HOH1181 |
| A | HOH1229 |
| A | LYS61 |
| A | ASN82 |
| A | LEU83 |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| A | VAL93 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CMO A 143 |
| Chain | Residue |
| A | HIS58 |
| A | VAL62 |
| A | HIS87 |
| A | HEM142 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 347 |
| Chain | Residue |
| B | THR238 |
| B | PHE241 |
| B | PHE242 |
| B | HIS263 |
| B | LYS266 |
| B | SER270 |
| B | LEU288 |
| B | HIS292 |
| B | LEU296 |
| B | ASN302 |
| B | PHE303 |
| B | LEU306 |
| B | LEU341 |
| B | CMO348 |
| B | HOH1051 |
| B | HOH1130 |
| B | HOH1180 |
| B | HOH1241 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CMO B 348 |
| Chain | Residue |
| B | HIS263 |
| B | VAL267 |
| B | HIS292 |
| B | HEM347 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PEM A 501 |
| Chain | Residue |
| A | ALA57 |
| A | LYS60 |
| A | LYS61 |
| A | ASP64 |
| A | ALA65 |
| A | LEU68 |
| A | HEM142 |
| A | HOH1001 |
| A | HOH1001 |
| A | HOH1053 |
| A | HOH1091 |
| A | HOH1273 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: distal binding residue => ECO:0000250|UniProtKB:P80044 |
| Chain | Residue | Details |
| B | HIS263 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: proximal binding residue => ECO:0000269|PubMed:561852, ECO:0007744|PDB:1G0B, ECO:0007744|PDB:1IBE, ECO:0007744|PDB:1IWH, ECO:0007744|PDB:1NS6, ECO:0007744|PDB:1NS9, ECO:0007744|PDB:1Y8H, ECO:0007744|PDB:1Y8I, ECO:0007744|PDB:1Y8K, ECO:0007744|PDB:2D5X, ECO:0007744|PDB:2DHB, ECO:0007744|PDB:2MHB, ECO:0007744|PDB:2ZLT, ECO:0007744|PDB:2ZLU, ECO:0007744|PDB:2ZLV, ECO:0007744|PDB:2ZLW, ECO:0007744|PDB:2ZLX |
| Chain | Residue | Details |
| B | HIS292 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086 |
| Chain | Residue | Details |
| B | VAL201 | |
| A | HIS50 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | SER244 | |
| A | ALA12 | |
| A | THR41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | LYS259 | |
| B | LYS282 | |
| B | LYS344 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | CYS293 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905 |
| Chain | Residue | Details |
| A | GLY25 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | HIS103 | |
| A | LEU125 | |
| A | VAL132 | |
| A | LYS139 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | LEU109 | |
| A | VAL135 | |
| A | SER138 |
