3H8L
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 | 28 |
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 | HOH411 |
A | HOH412 |
A | HOH419 |
A | HOH426 |
A | HOH469 |
A | PO42003 |
A | ARG10 |
A | PHE11 |
A | GLY12 |
A | ASN34 |
A | LYS35 |
A | ALA44 |
A | GLY76 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE S3H A 1002 |
Chain | Residue |
A | CYS178 |
A | LYS315 |
A | LEU316 |
A | CYS350 |
A | HOH550 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
Chain | Residue |
A | SER36 |
A | ARG37 |
A | GLU75 |
A | HOH521 |
A | HOH535 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 2002 |
Chain | Residue |
A | HIS190 |
A | LYS194 |
A | HOH525 |
B | LYS343 |
B | HOH476 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 2003 |
Chain | Residue |
A | LYS35 |
A | ALA111 |
A | HIS112 |
A | ASN271 |
A | PRO272 |
A | HOH426 |
A | HOH467 |
A | HOH488 |
A | HOH531 |
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 | HOH477 |
A | HOH482 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 B 2003 |
Chain | Residue |
B | ALA111 |
B | HIS112 |
B | PRO272 |
B | HOH425 |
B | HOH465 |
B | HOH488 |
B | HOH501 |
B | FAD1001 |
site_id | AC8 |
Number of Residues | 29 |
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 | HOH412 |
B | HOH413 |
B | HOH422 |
B | HOH436 |
B | HOH441 |
B | HOH465 |
B | PO42003 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE S3H B 1002 |
Chain | Residue |
B | CYS350 |
B | CYS178 |
B | LYS315 |
B | LEU316 |
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 | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 2002 |
Chain | Residue |
B | HIS190 |
B | LYS194 |
B | HOH487 |
B | HOH510 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 410 |
Chain | Residue |
A | LYS3 |
A | GLN72 |
B | GLU99 |
B | HOH444 |
B | HOH489 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 411 |
Chain | Residue |
A | TYR89 |
A | GLU99 |
B | LYS92 |
B | ASP94 |
B | SER96 |
B | HOH477 |
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 |