1QPW
CRYSTAL STRUCTURE DETERMINATION OF PORCINE HEMOGLOBIN AT 1.8A RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0015671 | biological_process | oxygen transport |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048821 | biological_process | erythrocyte development |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005515 | molecular_function | protein binding |
| 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 | 0031721 | molecular_function | hemoglobin alpha binding |
| B | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048821 | biological_process | erythrocyte development |
| C | 0005344 | molecular_function | oxygen carrier activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005833 | cellular_component | hemoglobin complex |
| C | 0015671 | biological_process | oxygen transport |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048821 | biological_process | erythrocyte development |
| D | 0005344 | molecular_function | oxygen carrier activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005833 | cellular_component | hemoglobin complex |
| D | 0015671 | biological_process | oxygen transport |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0031721 | molecular_function | hemoglobin alpha binding |
| D | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048821 | biological_process | erythrocyte development |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM A 650 |
| Chain | Residue |
| A | PHE43 |
| A | LEU101 |
| A | HOH754 |
| C | ALA12 |
| A | HIS45 |
| A | HIS58 |
| A | LYS61 |
| A | LEU83 |
| A | HIS87 |
| A | LEU91 |
| A | ASN97 |
| A | PHE98 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM B 750 |
| Chain | Residue |
| B | PHE41 |
| B | HIS63 |
| B | SER70 |
| B | LEU91 |
| B | HIS92 |
| B | LEU96 |
| B | ASN102 |
| B | LEU106 |
| B | LEU141 |
| B | OXY751 |
| B | HOH845 |
| B | HOH856 |
| C | HIS50 |
| D | HIS120 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OXY B 751 |
| Chain | Residue |
| B | HIS63 |
| B | HEM750 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM C 850 |
| Chain | Residue |
| C | TYR42 |
| C | PHE43 |
| C | HIS45 |
| C | HIS58 |
| C | LYS61 |
| C | LEU83 |
| C | HIS87 |
| C | LEU91 |
| C | VAL93 |
| C | ASN97 |
| C | PHE98 |
| C | LEU101 |
| C | OXY851 |
| D | HOH1136 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OXY C 851 |
| Chain | Residue |
| C | HIS58 |
| C | VAL62 |
| C | HEM850 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM D 950 |
| Chain | Residue |
| B | HOH837 |
| D | PHE41 |
| D | PHE42 |
| D | PHE45 |
| D | HIS63 |
| D | LYS66 |
| D | SER70 |
| D | LEU91 |
| D | HIS92 |
| D | LEU96 |
| D | VAL98 |
| D | ASN102 |
| D | LEU106 |
| D | LEU141 |
| D | HOH1142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: distal binding residue => ECO:0000250|UniProtKB:P80044 |
| Chain | Residue | Details |
| B | GLY64 | |
| D | GLY64 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:10713517, ECO:0000269|PubMed:7990139, ECO:0007744|PDB:1QPW, ECO:0007744|PDB:2PGH, ECO:0007744|PDB:4F4O |
| Chain | Residue | Details |
| B | CYS93 | |
| D | CYS93 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086 |
| Chain | Residue | Details |
| B | HIS2 | |
| D | HIS2 | |
| C | SER3 | |
| C | SER49 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | PHE45 | |
| D | PHE45 | |
| A | LYS40 | |
| C | LYS7 | |
| C | LYS11 | |
| C | LYS40 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | VAL60 | |
| B | GLY83 | |
| B | TYR145 | |
| D | VAL60 | |
| D | GLY83 | |
| D | TYR145 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | ASP94 | |
| D | ASP94 | |
| A | SER138 | |
| C | SER102 | |
| C | SER124 | |
| C | SER138 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | THR108 | |
| A | THR134 | |
| A | THR137 | |
| C | THR108 | |
| C | THR134 | |
| C | THR137 |
