6YAY
Crystal structure of a Selenium-derivatized complex of the bacterial cellulose secretion regulators BcsR and BcsQ, crystallized in the presence of ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0051782 | biological_process | negative regulation of cell division |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051782 | biological_process | negative regulation of cell division |
| C | 0030244 | biological_process | cellulose biosynthetic process |
| C | 0090540 | biological_process | bacterial cellulose biosynthetic process |
| D | 0030244 | biological_process | cellulose biosynthetic process |
| D | 0090540 | biological_process | bacterial cellulose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | THR16 |
| A | ATP302 |
| A | HOH408 |
| A | HOH409 |
| A | HOH416 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | binding site for residue ATP A 302 |
| Chain | Residue |
| A | THR15 |
| A | THR16 |
| A | THR17 |
| A | ASN171 |
| A | ASN172 |
| A | HIS200 |
| A | ARG201 |
| A | ASP202 |
| A | MSE205 |
| A | ALA206 |
| A | MG301 |
| A | HOH404 |
| A | HOH406 |
| A | HOH409 |
| A | HOH411 |
| A | HOH416 |
| B | ASP150 |
| B | ALA151 |
| B | ASN152 |
| B | ARG156 |
| A | GLY11 |
| A | GLY12 |
| A | VAL13 |
| A | GLY14 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | THR16 |
| B | ATP302 |
| B | HOH413 |
| B | HOH424 |
| B | HOH425 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue ATP B 302 |
| Chain | Residue |
| A | ASP150 |
| A | ALA151 |
| A | ASN152 |
| A | ARG156 |
| B | GLY11 |
| B | GLY12 |
| B | VAL13 |
| B | GLY14 |
| B | THR15 |
| B | THR16 |
| B | THR17 |
| B | ASN171 |
| B | ASN172 |
| B | HIS200 |
| B | ARG201 |
| B | ASP202 |
| B | MSE205 |
| B | ALA206 |
| B | MG301 |
| B | HOH401 |
| B | HOH403 |
| B | HOH405 |
| B | HOH413 |
| B | HOH424 |
| B | HOH429 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | VAL9 | |
| B | VAL9 |
