1Y01
Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0006457 | biological_process | protein folding |
| A | 0020027 | biological_process | hemoglobin metabolic process |
| A | 0030097 | biological_process | hemopoiesis |
| A | 0030218 | biological_process | erythrocyte differentiation |
| A | 0030492 | molecular_function | hemoglobin binding |
| A | 0050821 | biological_process | protein stabilization |
| A | 0051082 | molecular_function | unfolded protein binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEM B 142 |
| Chain | Residue |
| B | PHE43 |
| B | CHK144 |
| B | HOH150 |
| B | HIS58 |
| B | LYS61 |
| B | VAL62 |
| B | ALA65 |
| B | PHE98 |
| B | LEU101 |
| B | LEU136 |
| B | OXY143 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OXY B 143 |
| Chain | Residue |
| B | PHE98 |
| B | HEM142 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CHK B 144 |
| Chain | Residue |
| B | PHE33 |
| B | PHE43 |
| B | PHE46 |
| B | HIS58 |
| B | LYS61 |
| B | HEM142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 |
| Chain | Residue | Details |
| B | GLY59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238 |
| Chain | Residue | Details |
| B | ALA88 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | SITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433 |
| Chain | Residue | Details |
| B | ASN9 | |
| B | ARG92 | |
| B | VAL107 | |
| B | LEU109 | |
| B | HIS122 | |
| B | THR134 | |
| B | TRP14 | |
| B | GLY25 | |
| B | GLU30 | |
| B | PHE46 | |
| B | LEU48 | |
| B | ALA53 | |
| B | LYS56 | |
| B | LYS60 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | SITE: Not glycated => ECO:0000269|PubMed:7358733 |
| Chain | Residue | Details |
| B | ALA12 | |
| B | GLY57 | |
| B | LYS61 | |
| B | LEU91 | |
| B | LEU100 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | PRO4 | |
| B | PHE36 | |
| B | HIS50 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| B | THR8 | |
| B | VAL17 | |
| B | THR41 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | ASN9 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| B | ALA12 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | GLY25 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| B | HIS103 | |
| B | LEU125 | |
| B | VAL132 | |
| B | LYS139 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| B | LEU109 | |
| B | VAL135 | |
| B | SER138 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733 |
| Chain | Residue | Details |
| B | THR8 | |
| B | VAL17 | |
| B | THR41 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733 |
| Chain | Residue | Details |
| B | VAL62 |
