3C2W
Crystal structure of the photosensory core domain of P. aeruginosa bacteriophytochrome PaBphP in the Pfr state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0009584 | biological_process | detection of visible light |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0009584 | biological_process | detection of visible light |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0009584 | biological_process | detection of visible light |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0009584 | biological_process | detection of visible light |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0009584 | biological_process | detection of visible light |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0009584 | biological_process | detection of visible light |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0009584 | biological_process | detection of visible light |
H | 0006355 | biological_process | regulation of DNA-templated transcription |
H | 0009584 | biological_process | detection of visible light |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE BLA A 900 |
Chain | Residue |
A | CYS12 |
A | TYR203 |
A | ARG209 |
A | HIS247 |
A | TYR250 |
A | SER275 |
A | HIS277 |
A | HOH901 |
A | HOH905 |
A | GLU13 |
A | TYR163 |
A | GLN188 |
A | TYR190 |
A | SER193 |
A | ASP194 |
A | ILE195 |
A | PRO196 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BLA B 900 |
Chain | Residue |
B | CYS12 |
B | TYR163 |
B | GLN188 |
B | TYR190 |
B | ASP194 |
B | PRO196 |
B | TYR203 |
B | ARG209 |
B | SER244 |
B | HIS247 |
B | TYR250 |
B | SER259 |
B | SER275 |
B | HIS277 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BLA C 900 |
Chain | Residue |
C | CYS12 |
C | ILE17 |
C | TYR163 |
C | GLN188 |
C | TYR190 |
C | SER193 |
C | ASP194 |
C | PRO196 |
C | TYR203 |
C | ARG209 |
C | HIS247 |
C | TYR250 |
C | SER275 |
C | HIS277 |
C | ARG453 |
C | HOH901 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BLA D 900 |
Chain | Residue |
D | CYS12 |
D | GLU13 |
D | TYR163 |
D | GLN188 |
D | TYR190 |
D | ASP194 |
D | TYR203 |
D | ARG209 |
D | SER244 |
D | ILE246 |
D | HIS247 |
D | TYR250 |
D | SER275 |
D | HIS277 |
D | HOH902 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BLA E 900 |
Chain | Residue |
E | CYS12 |
E | TYR163 |
E | TYR185 |
E | TYR190 |
E | ASP194 |
E | PRO196 |
E | TYR203 |
E | ARG209 |
E | SER244 |
E | HIS247 |
E | TYR250 |
E | SER275 |
E | HIS277 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BLA F 900 |
Chain | Residue |
F | CYS12 |
F | TYR163 |
F | GLN188 |
F | ASP194 |
F | PRO196 |
F | TYR203 |
F | ARG209 |
F | ARG241 |
F | SER244 |
F | HIS247 |
F | TYR250 |
F | SER275 |
F | HOH901 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE BLA G 900 |
Chain | Residue |
G | HIS247 |
G | TYR250 |
G | SER275 |
G | HIS277 |
G | HOH901 |
G | HOH905 |
G | CYS12 |
G | TYR163 |
G | TYR185 |
G | GLN188 |
G | TYR190 |
G | ASP194 |
G | ILE195 |
G | PRO196 |
G | TYR203 |
G | ARG209 |
G | ILE211 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BLA H 900 |
Chain | Residue |
H | CYS12 |
H | TYR163 |
H | GLN188 |
H | TYR190 |
H | ASP194 |
H | TYR203 |
H | ARG209 |
H | ARG241 |
H | SER244 |
H | TYR250 |
H | SER275 |
H | HIS277 |
H | HOH902 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: covalent => ECO:0000250 |
Chain | Residue | Details |
A | CYS12 | |
B | CYS12 | |
C | CYS12 | |
D | CYS12 | |
E | CYS12 | |
F | CYS12 | |
G | CYS12 | |
H | CYS12 |