3IA3
A cis-proline in alpha-hemoglobin stabilizing Protein directs the structural reorganization of alpha-hemoglobin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006457 | biological_process | protein folding |
A | 0030218 | biological_process | erythrocyte differentiation |
A | 0030492 | molecular_function | hemoglobin binding |
A | 0050821 | biological_process | protein stabilization |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005344 | molecular_function | oxygen carrier activity |
B | 0005506 | molecular_function | iron ion binding |
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 | 0015670 | biological_process | carbon dioxide transport |
B | 0015671 | biological_process | oxygen transport |
B | 0016020 | cellular_component | membrane |
B | 0019825 | molecular_function | oxygen binding |
B | 0020037 | molecular_function | heme binding |
B | 0030185 | biological_process | nitric oxide transport |
B | 0031720 | molecular_function | haptoglobin 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 | 0046872 | molecular_function | metal ion binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 0071682 | cellular_component | endocytic vesicle lumen |
B | 0072562 | cellular_component | blood microparticle |
B | 0098869 | biological_process | cellular oxidant detoxification |
C | 0006457 | biological_process | protein folding |
C | 0030218 | biological_process | erythrocyte differentiation |
C | 0030492 | molecular_function | hemoglobin binding |
C | 0050821 | biological_process | protein stabilization |
D | 0004601 | molecular_function | peroxidase activity |
D | 0005344 | molecular_function | oxygen carrier activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0005829 | cellular_component | cytosol |
D | 0005833 | cellular_component | hemoglobin complex |
D | 0015670 | biological_process | carbon dioxide transport |
D | 0015671 | biological_process | oxygen transport |
D | 0016020 | cellular_component | membrane |
D | 0019825 | molecular_function | oxygen binding |
D | 0020037 | molecular_function | heme binding |
D | 0030185 | biological_process | nitric oxide transport |
D | 0031720 | molecular_function | haptoglobin binding |
D | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
D | 0042542 | biological_process | response to hydrogen peroxide |
D | 0042744 | biological_process | hydrogen peroxide catabolic process |
D | 0043177 | molecular_function | organic acid binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0070062 | cellular_component | extracellular exosome |
D | 0071682 | cellular_component | endocytic vesicle lumen |
D | 0072562 | cellular_component | blood microparticle |
D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM B 201 |
Chain | Residue |
B | PHE43 |
B | VAL93 |
B | ASN97 |
B | PHE98 |
B | LEU101 |
B | SER102 |
D | PRO77 |
D | ASN78 |
D | ALA79 |
B | HIS45 |
B | PHE46 |
B | HIS58 |
B | LYS61 |
B | VAL62 |
B | ALA65 |
B | LEU83 |
B | HIS87 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM D 201 |
Chain | Residue |
B | MET76 |
B | PRO77 |
B | ASN78 |
B | ALA79 |
D | PHE43 |
D | HIS45 |
D | PHE46 |
D | HIS58 |
D | LYS61 |
D | VAL62 |
D | ALA65 |
D | LEU83 |
D | HIS87 |
D | VAL93 |
D | ASN97 |
D | PHE98 |
D | LEU101 |
D | SER102 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 |
Chain | Residue | Details |
B | HIS58 | |
D | HIS58 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238 |
Chain | Residue | Details |
B | HIS87 | |
D | HIS87 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | SITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 |
Chain | Residue | Details |
B | THR8 | |
B | LEU91 | |
B | LEU106 | |
B | THR108 | |
B | VAL121 | |
B | SER133 | |
D | THR8 | |
D | ALA13 | |
D | TYR24 | |
D | LEU29 | |
D | HIS45 | |
B | ALA13 | |
D | ASP47 | |
D | SER52 | |
D | VAL55 | |
D | GLY59 | |
D | LEU91 | |
D | LEU106 | |
D | THR108 | |
D | VAL121 | |
D | SER133 | |
B | TYR24 | |
B | LEU29 | |
B | HIS45 | |
B | ASP47 | |
B | SER52 | |
B | VAL55 | |
B | GLY59 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | SITE: Not glycated => ECO:0000269|PubMed:7358733 |
Chain | Residue | Details |
B | LYS11 | |
D | LYS99 | |
B | LYS56 | |
B | LYS60 | |
B | LYS90 | |
B | LYS99 | |
D | LYS11 | |
D | LYS56 | |
D | LYS60 | |
D | LYS90 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | SER3 | |
B | SER35 | |
B | SER49 | |
D | SER3 | |
D | SER35 | |
D | SER49 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942 |
Chain | Residue | Details |
B | LYS7 | |
B | LYS16 | |
B | LYS40 | |
D | LYS7 | |
D | LYS16 | |
D | LYS40 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | THR8 | |
D | THR8 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942 |
Chain | Residue | Details |
B | LYS11 | |
D | LYS11 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
B | TYR24 | |
D | TYR24 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942 |
Chain | Residue | Details |
B | SER102 | |
B | SER124 | |
B | SER131 | |
B | SER138 | |
D | SER102 | |
D | SER124 | |
D | SER131 | |
D | SER138 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942 |
Chain | Residue | Details |
B | THR108 | |
B | THR134 | |
B | THR137 | |
D | THR108 | |
D | THR134 | |
D | THR137 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 |
Chain | Residue | Details |
B | LYS7 | |
B | LYS16 | |
B | LYS40 | |
D | LYS7 | |
D | LYS16 | |
D | LYS40 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 |
Chain | Residue | Details |
B | LYS61 | |
D | LYS61 |