3GYX
Crystal structure of adenylylsulfate reductase from Desulfovibrio gigas
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009973 | molecular_function | adenylyl-sulfate reductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019420 | biological_process | dissimilatory sulfate reduction |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0051290 | biological_process | protein heterotetramerization |
| A | 0071949 | molecular_function | FAD binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0019420 | biological_process | dissimilatory sulfate reduction |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0051290 | biological_process | protein heterotetramerization |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009973 | molecular_function | adenylyl-sulfate reductase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019420 | biological_process | dissimilatory sulfate reduction |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0051290 | biological_process | protein heterotetramerization |
| C | 0071949 | molecular_function | FAD binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0019420 | biological_process | dissimilatory sulfate reduction |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0051290 | biological_process | protein heterotetramerization |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009973 | molecular_function | adenylyl-sulfate reductase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0019420 | biological_process | dissimilatory sulfate reduction |
| E | 0046982 | molecular_function | protein heterodimerization activity |
| E | 0051290 | biological_process | protein heterotetramerization |
| E | 0071949 | molecular_function | FAD binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0019420 | biological_process | dissimilatory sulfate reduction |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0046982 | molecular_function | protein heterodimerization activity |
| F | 0051290 | biological_process | protein heterotetramerization |
| F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0005515 | molecular_function | protein binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0009973 | molecular_function | adenylyl-sulfate reductase activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0019420 | biological_process | dissimilatory sulfate reduction |
| G | 0046982 | molecular_function | protein heterodimerization activity |
| G | 0051290 | biological_process | protein heterotetramerization |
| G | 0071949 | molecular_function | FAD binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0019420 | biological_process | dissimilatory sulfate reduction |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0046982 | molecular_function | protein heterodimerization activity |
| H | 0051290 | biological_process | protein heterotetramerization |
| H | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0005515 | molecular_function | protein binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0009973 | molecular_function | adenylyl-sulfate reductase activity |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0019420 | biological_process | dissimilatory sulfate reduction |
| I | 0046982 | molecular_function | protein heterodimerization activity |
| I | 0051290 | biological_process | protein heterotetramerization |
| I | 0071949 | molecular_function | FAD binding |
| J | 0005515 | molecular_function | protein binding |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0019420 | biological_process | dissimilatory sulfate reduction |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0046982 | molecular_function | protein heterodimerization activity |
| J | 0051290 | biological_process | protein heterotetramerization |
| J | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| K | 0000166 | molecular_function | nucleotide binding |
| K | 0005515 | molecular_function | protein binding |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0009973 | molecular_function | adenylyl-sulfate reductase activity |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0019420 | biological_process | dissimilatory sulfate reduction |
| K | 0046982 | molecular_function | protein heterodimerization activity |
| K | 0051290 | biological_process | protein heterotetramerization |
| K | 0071949 | molecular_function | FAD binding |
| L | 0005515 | molecular_function | protein binding |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0019420 | biological_process | dissimilatory sulfate reduction |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0046982 | molecular_function | protein heterodimerization activity |
| L | 0051290 | biological_process | protein heterotetramerization |
| L | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD A 1000 |
| Chain | Residue |
| A | GLY31 |
| A | ALA69 |
| A | VAL70 |
| A | LEU74 |
| A | ALA76 |
| A | ASN78 |
| A | PHE192 |
| A | ILE193 |
| A | ALA230 |
| A | CYS231 |
| A | GLY232 |
| A | GLY32 |
| A | TRP251 |
| A | TYR252 |
| A | PRO253 |
| A | SER259 |
| A | MET385 |
| A | SER417 |
| A | HIS418 |
| A | ALA461 |
| A | ASP462 |
| A | PHE471 |
| A | GLY33 |
| A | SER472 |
| A | SER475 |
| A | MET34 |
| A | GLY35 |
| A | ASP60 |
| A | LYS61 |
| A | SER67 |
| A | GLY68 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 1000 |
| Chain | Residue |
| B | THR3 |
| B | CYS25 |
| B | ASN41 |
| B | CYS47 |
| B | GLU49 |
| B | CYS50 |
| B | TYR51 |
| B | CYS53 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 2000 |
| Chain | Residue |
| B | CYS10 |
| B | ASP11 |
| B | GLY12 |
| B | CYS13 |
| B | THR19 |
| B | CYS21 |
| B | ALA39 |
| B | CYS57 |
| B | ILE62 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD C 1000 |
| Chain | Residue |
| C | GLY32 |
| C | GLY33 |
| C | MET34 |
| C | GLY35 |
| C | ASP60 |
| C | LYS61 |
| C | SER67 |
| C | GLY68 |
| C | ALA69 |
| C | LEU74 |
| C | ALA76 |
| C | ASN78 |
| C | PHE192 |
| C | ILE193 |
| C | ALA230 |
| C | CYS231 |
| C | TRP251 |
| C | TYR252 |
| C | PRO253 |
| C | SER259 |
| C | SER417 |
| C | HIS418 |
| C | ALA461 |
| C | ASP462 |
| C | PHE471 |
| C | SER472 |
| C | SER475 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 D 1000 |
| Chain | Residue |
| D | THR3 |
| D | CYS25 |
| D | PRO26 |
| D | ASN41 |
| D | CYS47 |
| D | TRP48 |
| D | GLU49 |
| D | CYS50 |
| D | TYR51 |
| D | CYS53 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D 2000 |
| Chain | Residue |
| D | CYS10 |
| D | ASP11 |
| D | GLY12 |
| D | CYS13 |
| D | ALA20 |
| D | CYS21 |
| D | ALA39 |
| D | CYS57 |
| D | ILE62 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD E 1000 |
| Chain | Residue |
| E | ASP60 |
| E | LYS61 |
| E | SER67 |
| E | GLY68 |
| E | ALA69 |
| E | VAL70 |
| E | LEU74 |
| E | ALA76 |
| E | ILE77 |
| E | ASN78 |
| E | PHE192 |
| E | ILE193 |
| E | ALA230 |
| E | CYS231 |
| E | GLY232 |
| E | TRP251 |
| E | TYR252 |
| E | PRO253 |
| E | SER259 |
| E | SER417 |
| E | HIS418 |
| E | ALA461 |
| E | ASP462 |
| E | PHE471 |
| E | SER472 |
| E | SER475 |
| E | GLY31 |
| E | GLY32 |
| E | GLY33 |
| E | MET34 |
| E | GLY35 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 F 1000 |
| Chain | Residue |
| F | THR3 |
| F | CYS25 |
| F | PRO26 |
| F | MET30 |
| F | CYS47 |
| F | TRP48 |
| F | CYS50 |
| F | SER52 |
| F | CYS53 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 F 2000 |
| Chain | Residue |
| F | CYS10 |
| F | CYS13 |
| F | CYS21 |
| F | ALA39 |
| F | CYS57 |
| F | PRO58 |
| F | ILE62 |
| site_id | BC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD G 1000 |
| Chain | Residue |
| G | GLY31 |
| G | GLY32 |
| G | GLY33 |
| G | MET34 |
| G | GLY35 |
| G | ASP60 |
| G | LYS61 |
| G | SER67 |
| G | GLY68 |
| G | ALA69 |
| G | VAL70 |
| G | LEU74 |
| G | ALA76 |
| G | ILE77 |
| G | ASN78 |
| G | ILE191 |
| G | PHE192 |
| G | ILE193 |
| G | ALA230 |
| G | CYS231 |
| G | GLY232 |
| G | TRP251 |
| G | TYR252 |
| G | PRO253 |
| G | SER259 |
| G | MET385 |
| G | SER417 |
| G | HIS418 |
| G | ALA461 |
| G | ASP462 |
| G | PHE471 |
| G | SER472 |
| G | SER475 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 H 1000 |
| Chain | Residue |
| G | TRP255 |
| H | THR3 |
| H | CYS25 |
| H | PRO26 |
| H | ASN41 |
| H | CYS47 |
| H | CYS50 |
| H | TYR51 |
| H | CYS53 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 H 2000 |
| Chain | Residue |
| H | CYS10 |
| H | ASP11 |
| H | GLY12 |
| H | CYS13 |
| H | THR19 |
| H | ALA20 |
| H | CYS21 |
| H | CYS57 |
| H | PRO58 |
| H | GLN59 |
| H | ILE62 |
| site_id | BC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD I 1000 |
| Chain | Residue |
| I | GLY31 |
| I | GLY32 |
| I | GLY33 |
| I | MET34 |
| I | GLY35 |
| I | ASP60 |
| I | LYS61 |
| I | SER67 |
| I | GLY68 |
| I | ALA69 |
| I | VAL70 |
| I | LEU74 |
| I | ALA76 |
| I | ASN78 |
| I | ILE191 |
| I | PHE192 |
| I | ILE193 |
| I | ALA230 |
| I | CYS231 |
| I | GLY232 |
| I | TRP251 |
| I | TYR252 |
| I | PRO253 |
| I | SER259 |
| I | MET385 |
| I | SER417 |
| I | ALA461 |
| I | ASP462 |
| I | PHE471 |
| I | SER472 |
| I | SER475 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 J 1000 |
| Chain | Residue |
| J | THR3 |
| J | CYS25 |
| J | PRO26 |
| J | ASN41 |
| J | CYS47 |
| J | CYS50 |
| J | TYR51 |
| J | CYS53 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 J 2000 |
| Chain | Residue |
| J | CYS10 |
| J | ASP11 |
| J | GLY12 |
| J | CYS13 |
| J | THR19 |
| J | CYS21 |
| J | CYS57 |
| J | GLN59 |
| J | ILE62 |
| site_id | BC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD K 1000 |
| Chain | Residue |
| K | GLY31 |
| K | GLY32 |
| K | GLY33 |
| K | MET34 |
| K | GLY35 |
| K | ASP60 |
| K | LYS61 |
| K | SER67 |
| K | GLY68 |
| K | ALA69 |
| K | VAL70 |
| K | LEU74 |
| K | ALA76 |
| K | ASN78 |
| K | PHE192 |
| K | ILE193 |
| K | ALA230 |
| K | CYS231 |
| K | GLY232 |
| K | TRP251 |
| K | PRO253 |
| K | SER259 |
| K | SER417 |
| K | ALA461 |
| K | ASP462 |
| K | PHE471 |
| K | SER472 |
| K | SER475 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 L 1000 |
| Chain | Residue |
| L | THR3 |
| L | CYS25 |
| L | ASN41 |
| L | CYS47 |
| L | CYS50 |
| L | TYR51 |
| L | CYS53 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 L 2000 |
| Chain | Residue |
| L | VAL5 |
| L | CYS10 |
| L | GLY12 |
| L | CYS13 |
| L | THR19 |
| L | ALA20 |
| L | CYS21 |
| L | CYS57 |
| L | GLN59 |
| L | ILE62 |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CwECYsCIkICP |
| Chain | Residue | Details |
| B | CYS47-PRO58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19820092, ECO:0007744|PDB:3GYX |
| Chain | Residue | Details |
| B | CYS10 | |
| D | CYS13 | |
| D | CYS21 | |
| D | CYS25 | |
| D | CYS47 | |
| D | CYS50 | |
| D | CYS53 | |
| D | CYS57 | |
| F | CYS10 | |
| F | CYS13 | |
| F | CYS21 | |
| B | CYS13 | |
| F | CYS25 | |
| F | CYS47 | |
| F | CYS50 | |
| F | CYS53 | |
| F | CYS57 | |
| H | CYS10 | |
| H | CYS13 | |
| H | CYS21 | |
| H | CYS25 | |
| H | CYS47 | |
| B | CYS21 | |
| H | CYS50 | |
| H | CYS53 | |
| H | CYS57 | |
| J | CYS10 | |
| J | CYS13 | |
| J | CYS21 | |
| J | CYS25 | |
| J | CYS47 | |
| J | CYS50 | |
| J | CYS53 | |
| B | CYS25 | |
| J | CYS57 | |
| L | CYS10 | |
| L | CYS13 | |
| L | CYS21 | |
| L | CYS25 | |
| L | CYS47 | |
| L | CYS50 | |
| L | CYS53 | |
| L | CYS57 | |
| B | CYS47 | |
| B | CYS50 | |
| B | CYS53 | |
| B | CYS57 | |
| D | CYS10 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | SITE: Important for the electron transfer from the iron-sulfur cluster 1 to the FAD of AprA => ECO:0000305 |
| Chain | Residue | Details |
| B | TRP48 | |
| C | SER472 | |
| E | ASP60 | |
| E | SER259 | |
| E | SER417 | |
| E | ALA461 | |
| E | SER472 | |
| G | ASP60 | |
| G | SER259 | |
| G | SER417 | |
| G | ALA461 | |
| D | TRP48 | |
| G | SER472 | |
| I | ASP60 | |
| I | SER259 | |
| I | SER417 | |
| I | ALA461 | |
| I | SER472 | |
| K | ASP60 | |
| K | SER259 | |
| K | SER417 | |
| K | ALA461 | |
| F | TRP48 | |
| K | SER472 | |
| H | TRP48 | |
| J | TRP48 | |
| L | TRP48 | |
| C | SER259 | |
| C | SER417 | |
| C | ALA461 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | SITE: Important for interaction with AprA at the substrate channel entrance => ECO:0000269|PubMed:19820092 |
| Chain | Residue | Details |
| B | GLU152 | |
| H | GLU152 | |
| H | ASP159 | |
| H | GLU163 | |
| J | GLU152 | |
| J | ASP159 | |
| J | GLU163 | |
| L | GLU152 | |
| L | ASP159 | |
| L | GLU163 | |
| B | ASP159 | |
| B | GLU163 | |
| D | GLU152 | |
| D | ASP159 | |
| D | GLU163 | |
| F | GLU152 | |
| F | ASP159 | |
| F | GLU163 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | SITE: Important for interaction with AprB and for the binding of substrate at the substrate channel entrance => ECO:0000269|PubMed:19820092 |
| Chain | Residue | Details |
| A | ARG282 | |
| I | LYS300 | |
| K | ARG282 | |
| K | LYS300 | |
| A | LYS300 | |
| C | ARG282 | |
| C | LYS300 | |
| E | ARG282 | |
| E | LYS300 | |
| G | ARG282 | |
| G | LYS300 | |
| I | ARG282 |
