1E9V
XENON BOUND IN HYDROPHOBIC CHANNEL OF HYBRID CLUSTER PROTEIN FROM DESULFOVIBRIO VULGARIS
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FSO A 600 |
Chain | Residue |
A | HIS244 |
A | GLU268 |
A | ASN311 |
A | CYS312 |
A | CSS406 |
A | CYS434 |
A | CYS459 |
A | GLU494 |
A | LYS496 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SF4 A 650 |
Chain | Residue |
A | CYS3 |
A | PHE4 |
A | GLN5 |
A | CYS6 |
A | THR9 |
A | CYS15 |
A | GLY19 |
A | MET20 |
A | CYS21 |
A | LYS23 |
A | THR71 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE XE A 703 |
Chain | Residue |
A | LEU384 |
A | VAL388 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE XE A 705 |
Chain | Residue |
A | LEU501 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE XE A 706 |
Chain | Residue |
A | PHE400 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE XE A 707 |
Chain | Residue |
A | LEU430 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE XE A 709 |
Chain | Residue |
A | ILE490 |
A | ALA497 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE XE A 710 |
Chain | Residue |
A | ILE481 |
A | TYR488 |
A | LEU504 |
A | VAL509 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE XE A 711 |
Chain | Residue |
A | TRP492 |
A | LEU501 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE XE A 712 |
Chain | Residue |
A | SER462 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 800 |
Chain | Residue |
A | ASP76 |
A | TYR334 |
A | GLY336 |
A | ALA337 |
A | HOH2163 |
A | HOH2619 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS A 803 |
Chain | Residue |
A | THR227 |
A | ASN273 |
A | LYS279 |
A | PHE284 |
A | HOH2498 |
A | HOH2503 |
A | HOH2748 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY A 801 |
Chain | Residue |
A | GLU81 |
A | SER124 |
A | THR125 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 802 |
Chain | Residue |
A | GLU181 |
A | LYS201 |
A | HOH2746 |
A | HOH2747 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12, ECO:0000269|Ref.7 |
Chain | Residue | Details |
A | CYS3 | |
A | CYS6 | |
A | CYS15 | |
A | CYS21 |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12 |
Chain | Residue | Details |
A | HIS244 | |
A | GLU268 | |
A | CYS312 | |
A | CYS434 | |
A | CYS459 | |
A | GLU494 | |
A | LYS496 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: via persulfide group => ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12 |
Chain | Residue | Details |
A | CSS406 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine persulfide => ECO:0000269|PubMed:11941509 |
Chain | Residue | Details |
A | CSS406 |