6MRE
E. coli cysteine desulfurase SufS R92A with a cysteine persulfide intermediate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001887 | biological_process | selenium compound metabolic process |
A | 0003824 | molecular_function | catalytic activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006534 | biological_process | cysteine metabolic process |
A | 0006790 | biological_process | sulfur compound metabolic process |
A | 0008826 | molecular_function | cysteine sulfinate desulfinase activity |
A | 0009000 | molecular_function | selenocysteine lyase activity |
A | 0016226 | biological_process | iron-sulfur cluster assembly |
A | 0016740 | molecular_function | transferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0031071 | molecular_function | cysteine desulfurase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue PLP A 500 |
Chain | Residue |
A | THR94 |
A | LYS226 |
A | THR278 |
A | THR95 |
A | HIS123 |
A | ASN175 |
A | ASP200 |
A | ALA202 |
A | GLN203 |
A | SER223 |
A | HIS225 |
Functional Information from PROSITE/UniProt
site_id | PS00595 |
Number of Residues | 20 |
Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. CDFYvfSGHKlygpt.GiGiL |
Chain | Residue | Details |
A | CYS217-LEU236 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Cysteine persulfide intermediate |
Chain | Residue | Details |
A | CSS364 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS226 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 855 |
Chain | Residue | Details |
A | HIS123 | increase basicity, proton acceptor, proton donor |
A | ASP200 | electrostatic stabiliser, polar interaction |
A | GLN203 | electrostatic stabiliser, polar interaction |
A | LYS226 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | CSS364 | covalently attached, nucleophile, proton donor |