1GN9
Hybrid Cluster Protein from Desulfovibrio desulfuricans ATCC 27774 X-ray structure at 2.6A resolution using synchrotron radiation at a wavelength of 1.722A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050418 | molecular_function | hydroxylamine reductase activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| B | 0042542 | biological_process | response to hydrogen peroxide |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050418 | molecular_function | hydroxylamine reductase activity |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FSO A 600 |
| Chain | Residue |
| A | HIS240 |
| A | SER263 |
| A | GLU264 |
| A | TRP288 |
| A | CYS308 |
| A | CSS399 |
| A | CYS427 |
| A | CYS452 |
| A | GLU487 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 A 650 |
| Chain | Residue |
| A | MET4 |
| A | CYS6 |
| A | TYR7 |
| A | GLN8 |
| A | CYS9 |
| A | THR12 |
| A | CYS18 |
| A | GLY22 |
| A | VAL23 |
| A | CYS24 |
| A | THR75 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FSO B 600 |
| Chain | Residue |
| B | HIS240 |
| B | GLU264 |
| B | ASN307 |
| B | CYS308 |
| B | CSS399 |
| B | CYS427 |
| B | CYS452 |
| B | GLU487 |
| B | LYS489 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 650 |
| Chain | Residue |
| B | CYS6 |
| B | TYR7 |
| B | GLN8 |
| B | CYS9 |
| B | THR12 |
| B | CYS18 |
| B | GLY22 |
| B | VAL23 |
| B | CYS24 |
| B | THR75 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:14646063 |
| Chain | Residue | Details |
| A | TYR7 | |
| B | TYR7 | |
| B | GLN10 | |
| B | THR19 | |
| B | GLY25 | |
| B | ASP241 | |
| B | MET265 | |
| B | LEU309 | |
| B | ALA428 | |
| B | ASN453 | |
| A | GLN10 | |
| A | THR19 | |
| A | GLY25 | |
| A | ASP241 | |
| A | MET265 | |
| A | LEU309 | |
| A | ALA428 | |
| A | ASN453 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: via persulfide group => ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602 |
| Chain | Residue | Details |
| A | ASP400 | |
| B | ASP400 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:14646063 |
| Chain | Residue | Details |
| A | GLN488 | |
| A | ALA490 | |
| B | GLN488 | |
| B | ALA490 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Cysteine persulfide; in oxidized form => ECO:0000269|PubMed:11941509 |
| Chain | Residue | Details |
| A | ASP400 | |
| B | ASP400 |
