4UWQ
Crystal structure of the disulfide-linked complex of the thiosulfodyrolase SoxB with the carrier-protein SoxYZ from Thermus thermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0009166 | biological_process | nucleotide catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0009166 | biological_process | nucleotide catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0009166 | biological_process | nucleotide catabolic process |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0046872 | molecular_function | metal ion binding |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0009166 | biological_process | nucleotide catabolic process |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 580 |
| Chain | Residue |
| A | ASP47 |
| A | HIS49 |
| A | ASP143 |
| A | HIS299 |
| A | MN581 |
| B | GLY152 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 581 |
| Chain | Residue |
| A | HIS297 |
| A | MN580 |
| B | GLY152 |
| A | ASP143 |
| A | HIS174 |
| A | HIS274 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 580 |
| Chain | Residue |
| D | ASP47 |
| D | HIS49 |
| D | ASP143 |
| D | HIS299 |
| D | MN581 |
| E | GLY152 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 581 |
| Chain | Residue |
| D | ASP143 |
| D | HIS174 |
| D | HIS274 |
| D | HIS297 |
| D | MN580 |
| E | GLY152 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN G 580 |
| Chain | Residue |
| G | ASP47 |
| G | HIS49 |
| G | ASP143 |
| G | HIS299 |
| G | MN581 |
| H | GLY152 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN G 581 |
| Chain | Residue |
| G | ASP143 |
| G | HIS174 |
| G | HIS274 |
| G | HIS297 |
| G | MN580 |
| H | GLY152 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN J 580 |
| Chain | Residue |
| J | ASP47 |
| J | HIS49 |
| J | ASP143 |
| J | HIS299 |
| J | MN581 |
| K | GLY152 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN J 581 |
| Chain | Residue |
| J | ASP47 |
| J | ASP143 |
| J | HIS174 |
| J | HIS274 |
| J | HIS297 |
| J | MN580 |
| K | GLY152 |






