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 |