1JNZ
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6 resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000104 | molecular_function | succinate dehydrogenase activity |
A | 0000166 | molecular_function | nucleotide binding |
A | 0006113 | biological_process | fermentation |
A | 0009055 | molecular_function | electron transfer activity |
A | 0009061 | biological_process | anaerobic respiration |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
C | 0000104 | molecular_function | succinate dehydrogenase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0006113 | biological_process | fermentation |
C | 0009055 | molecular_function | electron transfer activity |
C | 0009061 | biological_process | anaerobic respiration |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO3 A 1001 |
Chain | Residue |
A | ASN74 |
A | TRP234 |
A | ARG265 |
A | MET365 |
A | HIS398 |
A | FAD1000 |
A | HOH5041 |
A | HOH7001 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO3 C 3001 |
Chain | Residue |
C | ARG2265 |
C | MET2365 |
C | HIS2398 |
C | FAD3000 |
C | HOH5001 |
C | ASN2074 |
site_id | AC3 |
Number of Residues | 40 |
Details | BINDING SITE FOR RESIDUE FAD A 1000 |
Chain | Residue |
A | GLY29 |
A | GLY31 |
A | PHE32 |
A | SER33 |
A | GLU56 |
A | LYS57 |
A | SER63 |
A | GLY64 |
A | ALA65 |
A | VAL66 |
A | LEU70 |
A | ALA72 |
A | ILE73 |
A | ASN74 |
A | VAL174 |
A | PHE175 |
A | ILE176 |
A | ALA213 |
A | THR214 |
A | GLY215 |
A | TRP234 |
A | TYR235 |
A | ALA236 |
A | ASP239 |
A | SER242 |
A | MET365 |
A | SER397 |
A | GLY438 |
A | ASP439 |
A | PHE448 |
A | SER449 |
A | SER452 |
A | SO31001 |
A | HOH5121 |
A | HOH5316 |
A | HOH5321 |
A | HOH5718 |
A | HOH7001 |
B | TRP748 |
B | HOH5045 |
site_id | AC4 |
Number of Residues | 42 |
Details | BINDING SITE FOR RESIDUE FAD C 3000 |
Chain | Residue |
C | GLY2029 |
C | GLY2030 |
C | GLY2031 |
C | PHE2032 |
C | SER2033 |
C | GLU2056 |
C | LYS2057 |
C | SER2063 |
C | GLY2064 |
C | ALA2065 |
C | VAL2066 |
C | LEU2070 |
C | ALA2072 |
C | ILE2073 |
C | ASN2074 |
C | VAL2174 |
C | PHE2175 |
C | ILE2176 |
C | ALA2213 |
C | THR2214 |
C | GLY2215 |
C | TRP2234 |
C | TYR2235 |
C | ALA2236 |
C | ASP2239 |
C | SER2242 |
C | MET2365 |
C | THR2366 |
C | SER2397 |
C | GLY2438 |
C | ASP2439 |
C | PHE2448 |
C | SER2449 |
C | SER2452 |
C | SO33001 |
C | HOH5008 |
C | HOH5048 |
C | HOH5059 |
C | HOH5197 |
C | HOH5320 |
C | HOH5621 |
D | TRP2748 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SF4 B 1100 |
Chain | Residue |
B | CYS747 |
B | TRP748 |
B | GLU749 |
B | CYS750 |
B | TYR751 |
B | SER752 |
B | CYS753 |
B | SER703 |
B | CYS725 |
B | ASN741 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 B 1110 |
Chain | Residue |
B | CYS710 |
B | ASP711 |
B | GLY712 |
B | CYS713 |
B | THR719 |
B | ALA720 |
B | CYS721 |
B | CYS757 |
B | ILE762 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 D 3100 |
Chain | Residue |
D | SER2703 |
D | CYS2725 |
D | PRO2726 |
D | CYS2747 |
D | TRP2748 |
D | CYS2750 |
D | TYR2751 |
D | CYS2753 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SF4 D 3110 |
Chain | Residue |
D | CYS2710 |
D | ASP2711 |
D | GLY2712 |
D | CYS2713 |
D | THR2719 |
D | ALA2720 |
D | CYS2721 |
D | CYS2757 |
D | GLN2759 |
D | ILE2762 |
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. CwECYsCVkMCP |
Chain | Residue | Details |
B | CYS747-PRO758 |