5IUL
Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000155 | molecular_function | phosphorelay sensor kinase activity |
A | 0000160 | biological_process | phosphorelay signal transduction system |
A | 0016020 | cellular_component | membrane |
A | 0046983 | molecular_function | protein dimerization activity |
B | 0000155 | molecular_function | phosphorelay sensor kinase activity |
B | 0000160 | biological_process | phosphorelay signal transduction system |
B | 0016020 | cellular_component | membrane |
B | 0046983 | molecular_function | protein dimerization activity |
C | 0000160 | biological_process | phosphorelay signal transduction system |
D | 0000155 | molecular_function | phosphorelay sensor kinase activity |
D | 0000160 | biological_process | phosphorelay signal transduction system |
D | 0016020 | cellular_component | membrane |
D | 0046983 | molecular_function | protein dimerization activity |
E | 0000155 | molecular_function | phosphorelay sensor kinase activity |
E | 0000160 | biological_process | phosphorelay signal transduction system |
E | 0016020 | cellular_component | membrane |
E | 0046983 | molecular_function | protein dimerization activity |
F | 0000160 | biological_process | phosphorelay signal transduction system |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue ACP A 401 |
Chain | Residue |
A | GLU289 |
A | GLY326 |
A | HIS335 |
A | GLY336 |
A | LEU337 |
A | THR359 |
A | MG402 |
A | HOH502 |
A | HOH503 |
A | ASN293 |
A | LYS296 |
A | HIS297 |
A | SER298 |
A | ASP320 |
A | THR323 |
A | PHE324 |
A | LYS325 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MG A 402 |
Chain | Residue |
A | GLU289 |
A | ASN293 |
A | ACP401 |
A | HOH502 |
site_id | AC3 |
Number of Residues | 17 |
Details | binding site for residue ACP B 401 |
Chain | Residue |
B | GLU289 |
B | ASN293 |
B | LYS296 |
B | HIS297 |
B | SER298 |
B | ASP320 |
B | THR323 |
B | PHE324 |
B | LYS325 |
B | GLY326 |
B | HIS335 |
B | GLY336 |
B | LEU337 |
B | THR359 |
B | MG402 |
B | HOH501 |
D | LYS312 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MG B 402 |
Chain | Residue |
B | GLU289 |
B | ASN293 |
B | ACP401 |
B | HOH501 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG C 201 |
Chain | Residue |
C | ASP9 |
C | ASP54 |
C | GLU56 |
C | HOH302 |
C | HOH304 |
C | HOH306 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue K C 202 |
Chain | Residue |
C | ASN22 |
C | GLU24 |
C | MET27 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue K C 203 |
Chain | Residue |
C | LEU69 |
C | LYS70 |
C | THR72 |
site_id | AC8 |
Number of Residues | 17 |
Details | binding site for residue ACP D 401 |
Chain | Residue |
D | GLU289 |
D | ASN293 |
D | LYS296 |
D | HIS297 |
D | SER298 |
D | ASP320 |
D | THR323 |
D | PHE324 |
D | LYS325 |
D | GLY326 |
D | HIS335 |
D | GLY336 |
D | LEU337 |
D | THR359 |
D | MG402 |
D | HOH501 |
D | HOH502 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue MG D 402 |
Chain | Residue |
D | GLU289 |
D | ASN293 |
D | ACP401 |
D | HOH501 |
site_id | AD1 |
Number of Residues | 17 |
Details | binding site for residue ACP E 401 |
Chain | Residue |
A | LYS312 |
E | GLU289 |
E | ASN293 |
E | LYS296 |
E | HIS297 |
E | SER298 |
E | ASP320 |
E | THR323 |
E | PHE324 |
E | LYS325 |
E | GLY326 |
E | HIS335 |
E | GLY336 |
E | LEU337 |
E | THR359 |
E | MG402 |
E | HOH501 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue MG E 402 |
Chain | Residue |
E | GLU289 |
E | ASN293 |
E | ACP401 |
E | HOH501 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue MG F 201 |
Chain | Residue |
F | HOH302 |
F | HOH303 |
F | HOH304 |
F | ASP9 |
F | ASP54 |
F | GLU56 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169 |
Chain | Residue | Details |
C | ASP54 | |
F | ASP54 | |
D | GLU188 | |
E | GLU188 |