4QTP
Crystal Structure of an Anti-sigma Factor Antagonist from Mycobacterium paratuberculosis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0043856 | molecular_function | anti-sigma factor antagonist activity |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0043856 | molecular_function | anti-sigma factor antagonist activity |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0043856 | molecular_function | anti-sigma factor antagonist activity |
C | 0045893 | biological_process | positive regulation of DNA-templated transcription |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0043856 | molecular_function | anti-sigma factor antagonist activity |
D | 0045893 | biological_process | positive regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CIT A 201 |
Chain | Residue |
A | GLY86 |
A | PRO87 |
A | ARG90 |
A | ARG91 |
A | HIS94 |
A | HOH353 |
D | ALA3 |
D | EDO203 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 202 |
Chain | Residue |
A | ALA3 |
A | SER6 |
A | THR8 |
A | SER23 |
A | GLY24 |
C | ALA33 |
C | EDO202 |
A | SER2 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 203 |
Chain | Residue |
A | SER2 |
A | GLU57 |
D | ARG91 |
D | HIS94 |
D | GOL204 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 204 |
Chain | Residue |
A | LYS65 |
A | ALA69 |
A | GOL205 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 205 |
Chain | Residue |
A | SER61 |
A | LYS65 |
A | EDO204 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CIT B 201 |
Chain | Residue |
B | GLY86 |
B | PRO87 |
B | ARG90 |
B | ARG91 |
B | HIS94 |
B | HOH325 |
B | HOH382 |
C | ALA3 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 202 |
Chain | Residue |
B | SER2 |
B | ALA3 |
B | SER6 |
B | THR8 |
B | SER23 |
B | GLY24 |
D | ALA33 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 203 |
Chain | Residue |
B | ASP99 |
B | LYS100 |
B | THR101 |
B | PHE102 |
B | HOH378 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 204 |
Chain | Residue |
B | SER61 |
B | LYS65 |
B | HOH398 |
site_id | BC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIT C 201 |
Chain | Residue |
B | LEU59 |
B | GLY60 |
B | SER61 |
B | PRO92 |
B | LEU95 |
B | THR96 |
B | HOH331 |
C | ASP27 |
C | MET28 |
C | PHE58 |
C | GLY60 |
C | SER61 |
C | VAL62 |
C | HOH302 |
C | HOH340 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 202 |
Chain | Residue |
A | SER2 |
A | EDO202 |
C | GLN36 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 203 |
Chain | Residue |
B | PRO87 |
C | PRO4 |
C | GLU25 |
C | GLU57 |
C | HOH355 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 204 |
Chain | Residue |
C | ASP99 |
C | LYS100 |
C | PHE102 |
C | PRO103 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO C 205 |
Chain | Residue |
C | HIS14 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 206 |
Chain | Residue |
C | ALA69 |
C | THR70 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 207 |
Chain | Residue |
C | LEU104 |
C | TYR105 |
C | HOH365 |
site_id | BC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIT D 201 |
Chain | Residue |
A | LEU59 |
A | GLY60 |
A | SER61 |
A | PRO92 |
A | LEU95 |
A | THR96 |
A | HOH335 |
D | ASP27 |
D | MET28 |
D | PHE58 |
D | GLY60 |
D | SER61 |
D | VAL62 |
D | HOH301 |
D | HOH337 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 202 |
Chain | Residue |
D | LYS73 |
D | HOH395 |
D | THR70 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 203 |
Chain | Residue |
A | PRO87 |
A | CIT201 |
D | GLU25 |
D | HOH327 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 204 |
Chain | Residue |
A | EDO203 |
D | ARG85 |
D | GLY86 |
D | PRO87 |
D | ARG90 |
D | ARG91 |