3H8I
The first X-ray structure of a sulfide:quinone oxidoreductase: Insights into sulfide oxidation mechanism
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0048038 | molecular_function | quinone binding |
| A | 0070224 | molecular_function | sulfide:quinone oxidoreductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0048038 | molecular_function | quinone binding |
| B | 0070224 | molecular_function | sulfide:quinone oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 1001 |
| Chain | Residue |
| A | GLY8 |
| A | THR77 |
| A | VAL78 |
| A | GLY108 |
| A | ILE109 |
| A | CYS129 |
| A | PRO181 |
| A | ASN271 |
| A | GLY306 |
| A | ASP307 |
| A | LYS315 |
| A | GLY9 |
| A | LEU316 |
| A | GLY317 |
| A | TYR318 |
| A | ALA320 |
| A | HOH411 |
| A | HOH412 |
| A | HOH418 |
| A | HOH420 |
| A | HOH436 |
| A | HOH475 |
| A | ARG10 |
| A | PO42003 |
| A | PHE11 |
| A | GLY12 |
| A | ASN34 |
| A | LYS35 |
| A | ALA44 |
| A | GLY76 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE S3H A 1002 |
| Chain | Residue |
| A | CYS178 |
| A | LYS315 |
| A | LEU316 |
| A | CYS350 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
| Chain | Residue |
| A | SER36 |
| A | ARG37 |
| A | GLU75 |
| A | HOH502 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2002 |
| Chain | Residue |
| A | HIS190 |
| A | LYS194 |
| A | LEU199 |
| A | GLN230 |
| B | LYS343 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2003 |
| Chain | Residue |
| A | ALA111 |
| A | HIS112 |
| A | ASN271 |
| A | PRO272 |
| A | HOH436 |
| A | HOH453 |
| A | HOH458 |
| A | HOH464 |
| A | FAD1001 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 410 |
| Chain | Residue |
| A | PRO155 |
| A | TYR157 |
| A | LYS240 |
| A | LYS240 |
| A | HOH454 |
| A | HOH461 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2003 |
| Chain | Residue |
| B | ALA111 |
| B | HIS112 |
| B | ASN271 |
| B | HOH426 |
| B | FAD1001 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 1001 |
| Chain | Residue |
| B | GLY8 |
| B | GLY9 |
| B | ARG10 |
| B | PHE11 |
| B | GLY12 |
| B | ASN34 |
| B | LYS35 |
| B | ALA44 |
| B | GLY76 |
| B | THR77 |
| B | VAL78 |
| B | GLY108 |
| B | ILE109 |
| B | CYS129 |
| B | PRO181 |
| B | ASN271 |
| B | GLY306 |
| B | ASP307 |
| B | LYS315 |
| B | LEU316 |
| B | GLY317 |
| B | TYR318 |
| B | ALA320 |
| B | HOH412 |
| B | HOH413 |
| B | HOH419 |
| B | HOH430 |
| B | PO42003 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE S3H B 1002 |
| Chain | Residue |
| B | CYS178 |
| B | LYS315 |
| B | LEU316 |
| B | CYS350 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2001 |
| Chain | Residue |
| B | SER36 |
| B | ARG37 |
| B | GLU75 |
| B | HOH460 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2002 |
| Chain | Residue |
| A | HOH487 |
| B | HIS190 |
| B | LYS194 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 410 |
| Chain | Residue |
| A | LYS3 |
| A | GLN72 |
| B | SER85 |
| B | TYR89 |
| B | GLU99 |
| B | HOH445 |
| B | HOH452 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 411 |
| Chain | Residue |
| A | TYR89 |
| B | LYS92 |
| B | ASP94 |
| B | HOH449 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Cysteine persulfide intermediate => ECO:0000269|PubMed:19438211 |
| Chain | Residue | Details |
| A | CYS178 | |
| A | CYS350 | |
| B | CYS178 | |
| B | CYS350 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19438211 |
| Chain | Residue | Details |
| A | GLY8 | |
| B | ASN271 | |
| B | ASP307 | |
| B | GLY317 | |
| A | ASN34 | |
| A | CYS129 | |
| A | ASN271 | |
| A | ASP307 | |
| A | GLY317 | |
| B | GLY8 | |
| B | ASN34 | |
| B | CYS129 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 320 |
| Chain | Residue | Details |
| A | CYS129 | activator, covalently attached |
| A | CYS178 | activator, covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| A | ASP215 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | CYS350 | activator, covalently attached, electrofuge, electrophile |
| A | ASP353 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | LYS386 | activator |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 320 |
| Chain | Residue | Details |
| B | CYS129 | activator, covalently attached |
| B | CYS178 | activator, covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| B | ASP215 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | CYS350 | activator, covalently attached, electrofuge, electrophile |
| B | ASP353 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | LYS386 | activator |
