3SZC
Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans in complex with gold (I) cyanide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019646 | biological_process | aerobic electron transport chain |
| A | 0048038 | molecular_function | quinone binding |
| A | 0070224 | molecular_function | sulfide:quinone oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD A 500 |
| Chain | Residue |
| A | LEU7 |
| A | VAL42 |
| A | SER77 |
| A | ALA78 |
| A | ALA104 |
| A | THR105 |
| A | GLY106 |
| A | PRO107 |
| A | ILE127 |
| A | PRO163 |
| A | VAL267 |
| A | GLY8 |
| A | GLY301 |
| A | ILE302 |
| A | LYS320 |
| A | THR321 |
| A | GLY322 |
| A | VAL355 |
| A | CYS356 |
| A | PHE357 |
| A | LYS391 |
| A | DCQ502 |
| A | ALA9 |
| A | AU503 |
| A | H2S508 |
| A | HOH510 |
| A | HOH514 |
| A | HOH523 |
| A | HOH527 |
| A | HOH529 |
| A | GLY10 |
| A | THR11 |
| A | GLY12 |
| A | SER34 |
| A | ALA35 |
| A | ASN36 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DCQ A 502 |
| Chain | Residue |
| A | THR11 |
| A | PRO43 |
| A | GLY322 |
| A | TYR323 |
| A | PHE357 |
| A | LYS391 |
| A | PHE394 |
| A | TYR411 |
| A | LYS413 |
| A | LYS417 |
| A | FAD500 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE AU A 503 |
| Chain | Residue |
| A | CYS128 |
| A | FAD500 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE AU A 504 |
| Chain | Residue |
| A | CYS160 |
| A | LYS320 |
| A | AU505 |
| A | H2S509 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE AU A 505 |
| Chain | Residue |
| A | CYS160 |
| A | AU504 |
| A | H2S506 |
| A | H2S508 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE H2S A 506 |
| Chain | Residue |
| A | GLY162 |
| A | CYS356 |
| A | AU505 |
| A | H2S508 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | MET-2 |
| A | HIS3 |
| A | HIS97 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE H2S A 508 |
| Chain | Residue |
| A | CYS356 |
| A | FAD500 |
| A | AU505 |
| A | H2S506 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S A 509 |
| Chain | Residue |
| A | SER159 |
| A | PHE264 |
| A | LYS320 |
| A | AU504 |
| A | HOH513 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"20303979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22542586","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20303979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22542586","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
