Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005829 | cellular_component | cytosol |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0009000 | molecular_function | selenocysteine lyase activity |
A | 0016261 | biological_process | selenocysteine catabolic process |
A | 0016597 | molecular_function | amino acid binding |
A | 0016740 | molecular_function | transferase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0070279 | molecular_function | vitamin B6 binding |
A | 1902494 | cellular_component | catalytic complex |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0005829 | cellular_component | cytosol |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0009000 | molecular_function | selenocysteine lyase activity |
B | 0016261 | biological_process | selenocysteine catabolic process |
B | 0016597 | molecular_function | amino acid binding |
B | 0016740 | molecular_function | transferase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0070279 | molecular_function | vitamin B6 binding |
B | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLR A 500 |
Chain | Residue |
A | GLY99 |
A | LYS259 |
A | HOH461 |
A | HOH470 |
A | HOH596 |
B | THR296 |
A | THR100 |
A | HIS145 |
A | SER147 |
A | ASP233 |
A | ALA235 |
A | GLN236 |
A | VAL256 |
A | HIS258 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLR B 500 |
Chain | Residue |
A | THR296 |
B | GLY99 |
B | THR100 |
B | HIS145 |
B | SER147 |
B | ASP233 |
B | ALA235 |
B | GLN236 |
B | HIS258 |
B | LYS259 |
B | HOH459 |
B | HOH569 |
B | HOH666 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"S-selanylcysteine intermediate","evidences":[{"source":"UniProtKB","id":"Q68FT9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2006","submissionDatabase":"PDB data bank","title":"Structure of human selenocysteine lyase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
A | PHE138 | |
A | ASP233 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
B | PHE138 | |
B | ASP233 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
A | LYS259 | |
A | HIS145 | |
A | ASP233 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
B | LYS259 | |
B | HIS145 | |
B | ASP233 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
A | CYS388 | |
A | LYS259 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
B | CYS388 | |
B | LYS259 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
A | ARG69 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ax4 |
Chain | Residue | Details |
B | ARG69 |