Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005344 | molecular_function | oxygen carrier activity |
A | 0015671 | biological_process | oxygen transport |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016528 | cellular_component | sarcoplasm |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0019825 | molecular_function | oxygen binding |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0098809 | molecular_function | nitrite reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM A 201 |
Chain | Residue |
A | LYS42 |
A | ILE99 |
A | TYR103 |
A | OXY202 |
A | DMS203 |
A | HOH332 |
A | HOH362 |
A | HOH381 |
A | HOH474 |
A | HOH476 |
A | HOH477 |
A | PHE43 |
A | HOH478 |
A | HOH490 |
A | ARG45 |
A | HIS64 |
A | VAL68 |
A | LEU89 |
A | SER92 |
A | HIS93 |
A | HIS97 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE OXY A 202 |
Chain | Residue |
A | HIS64 |
A | VAL68 |
A | HEM201 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 203 |
Chain | Residue |
A | LEU89 |
A | HIS93 |
A | LEU104 |
A | PHE138 |
A | HEM201 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 204 |
Chain | Residue |
A | GLY124 |
A | ALA125 |
A | ASP126 |
A | HOH479 |
A | HOH482 |
A | HOH483 |
A | HOH484 |
A | HOH566 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 205 |
Chain | Residue |
A | SER3 |
A | GLU4 |
A | THR51 |
A | GLU52 |
A | ALA53 |
A | HOH314 |
A | HOH495 |
A | HOH496 |
A | HOH508 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 206 |
Chain | Residue |
A | SER3 |
A | GLY5 |
A | HOH314 |
A | HOH317 |
A | HOH318 |
A | HOH508 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 207 |
Chain | Residue |
A | ARG45 |
A | HIS64 |
A | THR67 |
A | HOH476 |
A | HOH489 |
A | HOH553 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 208 |
Chain | Residue |
A | THR95 |
A | GLU109 |
A | LEU149 |
A | GLY150 |
A | HOH426 |
A | HOH499 |
A | HOH523 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 146 |
Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7463482","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MBO","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"845959","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MBN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MBN","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QZ76","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04247","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |