2D5X
Crystal structure of carbonmonoxy horse hemoglobin complexed with L35
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 | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 142 |
| Chain | Residue |
| A | TYR42 |
| A | ASN97 |
| A | PHE98 |
| A | LEU101 |
| A | LEU136 |
| A | CMO1143 |
| A | L351200 |
| A | HOH1248 |
| A | HOH1258 |
| A | HOH1263 |
| A | PHE43 |
| A | HIS58 |
| A | LYS61 |
| A | LEU83 |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| A | VAL93 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CMO A 1143 |
| Chain | Residue |
| A | LEU29 |
| A | HIS58 |
| A | VAL62 |
| A | HEM142 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 147 |
| Chain | Residue |
| B | THR38 |
| B | PHE41 |
| B | PHE42 |
| B | HIS63 |
| B | LYS66 |
| B | SER70 |
| B | PHE71 |
| B | LEU88 |
| B | HIS92 |
| B | LEU96 |
| B | VAL98 |
| B | ASN102 |
| B | PHE103 |
| B | LEU106 |
| B | LEU141 |
| B | CMO1148 |
| B | HOH1228 |
| B | HOH1254 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO B 1148 |
| Chain | Residue |
| B | HIS63 |
| B | VAL67 |
| B | HEM147 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE L35 A 1200 |
| Chain | Residue |
| A | LEU68 |
| A | ASN82 |
| A | ASN82 |
| A | LEU83 |
| A | ASP85 |
| A | LEU86 |
| A | LYS90 |
| A | HEM142 |
| A | HOH1263 |
| A | HOH1305 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE L35 B 1201 |
| Chain | Residue |
| A | LYS99 |
| A | LEU100 |
| A | HIS103 |
| A | SER130 |
| A | THR137 |
| A | HOH1229 |
| A | HOH1243 |
| B | TYR35 |
| B | TRP37 |
| B | LEU105 |
| B | ASN108 |
| B | HOH1234 |
| B | HOH1287 |
| B | HOH1301 |
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 | HIS63 |
| 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 | HIS92 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086 |
| Chain | Residue | Details |
| B | VAL1 | |
| A | HIS50 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | SER44 | |
| 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 | LYS59 | |
| B | LYS82 | |
| B | LYS144 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | CYS93 |
| 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 |
