3SY4
Crystal structure of sulfide:quinone oxidoreductase Ser126Ala variant from Acidithiobacillus ferrooxidans
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 | 42 |
| Details | BINDING SITE FOR RESIDUE FAD A 500 |
| Chain | Residue |
| A | LEU7 |
| A | VAL42 |
| A | PRO43 |
| A | SER77 |
| A | ALA78 |
| A | ALA104 |
| A | THR105 |
| A | GLY106 |
| A | PRO107 |
| A | CYS160 |
| A | PRO163 |
| A | GLY8 |
| A | VAL267 |
| A | GLY301 |
| A | ILE302 |
| A | LYS320 |
| A | THR321 |
| A | GLY322 |
| A | ILE325 |
| A | VAL355 |
| A | PHE357 |
| A | LYS391 |
| A | ALA9 |
| A | H2S505 |
| A | HOH508 |
| A | HOH509 |
| A | HOH530 |
| A | HOH543 |
| A | HOH560 |
| A | HOH567 |
| A | HOH612 |
| A | HOH645 |
| A | HOH700 |
| A | GLY10 |
| A | HOH701 |
| A | HOH792 |
| A | HOH801 |
| A | THR11 |
| A | GLY12 |
| A | SER34 |
| A | ALA35 |
| A | ASN36 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE LMT A 501 |
| Chain | Residue |
| A | GLY162 |
| A | MET169 |
| A | GLY205 |
| A | ASP206 |
| A | ILE210 |
| A | LEU211 |
| A | GLU217 |
| A | CYS356 |
| A | ALA358 |
| A | ALA365 |
| A | PHE367 |
| A | TYR383 |
| A | HOH518 |
| A | HOH562 |
| A | HOH620 |
| A | HOH672 |
| A | HOH738 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S A 502 |
| Chain | Residue |
| A | GLY162 |
| A | CYS356 |
| A | H2S504 |
| A | H2S505 |
| A | HOH706 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S A 503 |
| Chain | Residue |
| A | LEU109 |
| A | ALA126 |
| A | CYS128 |
| A | THR129 |
| A | HIS132 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE H2S A 504 |
| Chain | Residue |
| A | CYS160 |
| A | H2S502 |
| A | H2S505 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE H2S A 505 |
| Chain | Residue |
| A | CYS356 |
| A | FAD500 |
| A | H2S502 |
| A | H2S504 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE H2S A 506 |
| Chain | Residue |
| A | LYS374 |
| A | PRO375 |
| A | ARG376 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | MET-2 |
| A | HIS3 |
| A | HIS97 |
| A | HOH676 |
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 |
