3A9X
Crystal structure of rat selenocysteine lyase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001887 | biological_process | selenium compound metabolic process |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid 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 | 0032868 | biological_process | response to insulin |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0070279 | molecular_function | vitamin B6 binding |
| A | 1900408 | biological_process | negative regulation of cellular response to oxidative stress |
| A | 1902494 | cellular_component | catalytic complex |
| B | 0001887 | biological_process | selenium compound metabolic process |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid 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 | 0032868 | biological_process | response to insulin |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0070279 | molecular_function | vitamin B6 binding |
| B | 1900408 | biological_process | negative regulation of cellular response to oxidative stress |
| B | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | GLY87 |
| A | LYS247 |
| A | HOH444 |
| A | HOH445 |
| B | GLY283 |
| B | THR284 |
| B | HOH514 |
| A | THR88 |
| A | ASN91 |
| A | HIS133 |
| A | ASN186 |
| A | ASP221 |
| A | ALA223 |
| A | GLN224 |
| A | HIS246 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 501 |
| Chain | Residue |
| A | GLY283 |
| A | THR284 |
| B | GLY87 |
| B | THR88 |
| B | HIS133 |
| B | ASP221 |
| B | ALA223 |
| B | GLN224 |
| B | HIS246 |
| B | LYS247 |
| B | HOH439 |
| B | PO4502 |
| B | PO4503 |
| B | HOH535 |
| B | HOH617 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 502 |
| Chain | Residue |
| A | ASN48 |
| A | THR284 |
| B | ALA26 |
| B | HIS133 |
| B | LYS247 |
| B | SER374 |
| B | CYS375 |
| B | PLP501 |
| B | PO4503 |
| B | HOH617 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 503 |
| Chain | Residue |
| B | ASN25 |
| B | ALA26 |
| B | ASN186 |
| B | GLN224 |
| B | LYS247 |
| B | ALA373 |
| B | SER374 |
| B | ARG402 |
| B | PLP501 |
| B | PO4502 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 504 |
| Chain | Residue |
| B | ARG315 |
| B | ASP316 |
| B | ARG341 |
| B | GLY352 |
| B | SER353 |
| B | GLU429 |
| B | HOH497 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20164179","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3A9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A9Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"S-selanylcysteine intermediate","evidences":[{"source":"PubMed","id":"20164179","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
