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 | 0005737 | cellular_component | cytoplasm |
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 | 0005737 | cellular_component | cytoplasm |
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 | ACT_SITE: S-selanylcysteine intermediate => ECO:0000269|PubMed:20164179 |
Chain | Residue | Details |
A | CYS375 | |
B | CYS375 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q96I15 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q96I15 |
Chain | Residue | Details |
A | SER117 | |
B | SER117 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20164179, ECO:0007744|PDB:3A9X, ECO:0007744|PDB:3A9Y, ECO:0007744|PDB:3A9Z |
Chain | Residue | Details |
A | LYS247 | |
B | LYS247 |