3T2Z
Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans
Replaces: 3KPIFunctional 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019646 | biological_process | aerobic electron transport chain |
| 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 | 40 |
| Details | BINDING SITE FOR RESIDUE FAD A 500 |
| Chain | Residue |
| A | LEU7 |
| A | PRO43 |
| A | SER77 |
| A | ALA78 |
| A | ALA104 |
| A | THR105 |
| A | GLY106 |
| A | PRO107 |
| A | CYS160 |
| A | PRO163 |
| A | GLY301 |
| A | GLY8 |
| A | ILE302 |
| A | THR321 |
| A | GLY322 |
| A | ILE325 |
| A | VAL355 |
| A | PHE357 |
| A | LYS391 |
| A | S3H442 |
| A | H2S443 |
| A | HOH465 |
| A | ALA9 |
| A | BU2502 |
| A | HOH515 |
| A | HOH526 |
| A | HOH542 |
| A | HOH555 |
| A | HOH614 |
| A | HOH618 |
| A | HOH685 |
| A | HOH702 |
| A | HOH734 |
| A | GLY10 |
| A | HOH758 |
| A | THR11 |
| A | GLY12 |
| A | SER34 |
| A | ALA35 |
| A | VAL42 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BU2 A 502 |
| Chain | Residue |
| A | PRO43 |
| A | VAL355 |
| A | PHE357 |
| A | LYS391 |
| A | PHE394 |
| A | MET418 |
| A | FAD500 |
| A | HOH531 |
| A | HOH548 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 435 |
| Chain | Residue |
| A | TYR397 |
| A | ARG400 |
| A | LYS401 |
| A | LYS413 |
| A | LYS417 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 436 |
| Chain | Residue |
| A | HIS334 |
| A | ARG343 |
| A | LYS344 |
| A | GLY345 |
| A | GLU346 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 437 |
| Chain | Residue |
| A | LYS401 |
| A | VAL406 |
| A | SER407 |
| A | PRO409 |
| A | PHE410 |
| A | LYS413 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 438 |
| Chain | Residue |
| A | TYR195 |
| A | HIS198 |
| A | GLN202 |
| A | GLU310 |
| A | HOH752 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 439 |
| Chain | Residue |
| A | ARG63 |
| A | ILE74 |
| A | ALA75 |
| A | GLN76 |
| B | HIS72 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S A 440 |
| Chain | Residue |
| A | LEU109 |
| A | SER126 |
| A | CYS128 |
| A | THR129 |
| A | HIS132 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE S3H A 442 |
| Chain | Residue |
| A | CYS160 |
| A | CYS356 |
| A | H2S441 |
| A | H2S445 |
| A | FAD500 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE H2S A 441 |
| Chain | Residue |
| A | PRO163 |
| A | GLU166 |
| A | CYS356 |
| A | PHE357 |
| A | S3H442 |
| A | HOH532 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE H2S A 443 |
| Chain | Residue |
| A | CYS356 |
| A | H2S444 |
| A | H2S445 |
| A | FAD500 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE H2S A 444 |
| Chain | Residue |
| A | CYS160 |
| A | PRO319 |
| A | H2S443 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S A 445 |
| Chain | Residue |
| A | CYS356 |
| A | S3H442 |
| A | H2S443 |
| A | HOH620 |
| A | GLY162 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BU2 B 501 |
| Chain | Residue |
| B | PHE41 |
| B | PRO43 |
| B | VAL355 |
| B | CYS356 |
| B | PHE357 |
| B | LYS391 |
| B | PHE394 |
| B | MET418 |
| B | FAD500 |
| B | HOH617 |
| site_id | BC6 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD B 500 |
| Chain | Residue |
| B | LEU7 |
| B | GLY8 |
| B | ALA9 |
| B | GLY10 |
| B | THR11 |
| B | GLY12 |
| B | SER34 |
| B | ALA35 |
| B | VAL42 |
| B | PRO43 |
| B | SER77 |
| B | ALA78 |
| B | ALA104 |
| B | THR105 |
| B | GLY106 |
| B | PRO107 |
| B | CYS128 |
| B | CYS160 |
| B | PRO163 |
| B | GLY301 |
| B | ILE302 |
| B | THR321 |
| B | GLY322 |
| B | ILE325 |
| B | VAL355 |
| B | PHE357 |
| B | LYS391 |
| B | S3H442 |
| B | H2S443 |
| B | HOH450 |
| B | HOH474 |
| B | HOH489 |
| B | HOH494 |
| B | BU2501 |
| B | HOH608 |
| B | HOH656 |
| B | HOH661 |
| B | HOH726 |
| B | HOH759 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 435 |
| Chain | Residue |
| B | TYR397 |
| B | ARG400 |
| B | LYS401 |
| B | LYS413 |
| B | LYS417 |
| B | ARG423 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 436 |
| Chain | Residue |
| A | HIS72 |
| A | HOH716 |
| B | ASP37 |
| B | ARG63 |
| B | ALA75 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 437 |
| Chain | Residue |
| B | HIS334 |
| B | ARG343 |
| B | LYS344 |
| B | GLY345 |
| B | GLU346 |
| B | GLN347 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 438 |
| Chain | Residue |
| B | TYR195 |
| B | HIS198 |
| B | GLN202 |
| B | GLU310 |
| B | HOH540 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 439 |
| Chain | Residue |
| B | LYS401 |
| B | VAL406 |
| B | SER407 |
| B | PHE410 |
| B | LYS413 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 440 |
| Chain | Residue |
| B | LYS176 |
| B | GLY179 |
| B | MET180 |
| B | ARG181 |
| B | ASP182 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S B 441 |
| Chain | Residue |
| B | LEU109 |
| B | SER126 |
| B | CYS128 |
| B | THR129 |
| B | HIS132 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE S3H B 442 |
| Chain | Residue |
| B | CYS160 |
| B | CYS356 |
| B | H2S445 |
| B | H2S447 |
| B | FAD500 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S B 443 |
| Chain | Residue |
| B | THR321 |
| B | CYS356 |
| B | H2S444 |
| B | H2S445 |
| B | FAD500 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE H2S B 444 |
| Chain | Residue |
| B | CYS160 |
| B | H2S443 |
| B | FAD500 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S B 445 |
| Chain | Residue |
| B | GLY162 |
| B | CYS356 |
| B | S3H442 |
| B | H2S443 |
| B | HOH619 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE H2S B 447 |
| Chain | Residue |
| B | PRO163 |
| B | GLU166 |
| B | CYS356 |
| B | PHE357 |
| B | S3H442 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20303979","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22542586","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
