3HUG
Crystal structure of Mycobacterium tuberculosis anti-sigma factor RslA in complex with -35 promoter binding domain of sigL
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0006352 | biological_process | DNA-templated transcription initiation |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0003700 | molecular_function | DNA-binding transcription factor activity |
C | 0006352 | biological_process | DNA-templated transcription initiation |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0003700 | molecular_function | DNA-binding transcription factor activity |
E | 0006352 | biological_process | DNA-templated transcription initiation |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0003700 | molecular_function | DNA-binding transcription factor activity |
G | 0006352 | biological_process | DNA-templated transcription initiation |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
I | 0003700 | molecular_function | DNA-binding transcription factor activity |
I | 0006352 | biological_process | DNA-templated transcription initiation |
I | 0006355 | biological_process | regulation of DNA-templated transcription |
K | 0003700 | molecular_function | DNA-binding transcription factor activity |
K | 0006352 | biological_process | DNA-templated transcription initiation |
K | 0006355 | biological_process | regulation of DNA-templated transcription |
M | 0003700 | molecular_function | DNA-binding transcription factor activity |
M | 0006352 | biological_process | DNA-templated transcription initiation |
M | 0006355 | biological_process | regulation of DNA-templated transcription |
O | 0003700 | molecular_function | DNA-binding transcription factor activity |
O | 0006352 | biological_process | DNA-templated transcription initiation |
O | 0006355 | biological_process | regulation of DNA-templated transcription |
Q | 0003700 | molecular_function | DNA-binding transcription factor activity |
Q | 0006352 | biological_process | DNA-templated transcription initiation |
Q | 0006355 | biological_process | regulation of DNA-templated transcription |
S | 0003700 | molecular_function | DNA-binding transcription factor activity |
S | 0006352 | biological_process | DNA-templated transcription initiation |
S | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 Q 1 |
Chain | Residue |
I | GLN101 |
I | SER102 |
Q | HOH27 |
Q | ARG137 |
R | ARG76 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 L 109 |
Chain | Residue |
L | ARG76 |
C | GLN101 |
C | SER102 |
K | GLN132 |
K | ARG137 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 3 |
Chain | Residue |
A | GLN132 |
A | ARG137 |
B | ARG76 |
B | ALA80 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 M 4 |
Chain | Residue |
M | GLN132 |
M | ARG137 |
N | ARG76 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 5 |
Chain | Residue |
C | GLN132 |
C | ARG137 |
C | HOH183 |
D | ARG76 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 G 6 |
Chain | Residue |
G | GLN132 |
G | ARG137 |
H | ARG76 |
H | ALA80 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 S 7 |
Chain | Residue |
S | GLN132 |
S | ARG137 |
T | ARG76 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 P 109 |
Chain | Residue |
O | ARG137 |
P | ARG76 |
P | ALA80 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 I 9 |
Chain | Residue |
I | GLN132 |
I | ARG137 |
J | ARG76 |
Q | GLN101 |
Q | SER102 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 I 10 |
Chain | Residue |
I | ARG113 |
I | LEU114 |
Q | ARG113 |
Q | LEU114 |
Q | ALA117 |
R | LEU74 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 109 |
Chain | Residue |
B | HIS25 |
B | HIS50 |
B | CYS54 |
B | CYS57 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 109 |
Chain | Residue |
D | HIS25 |
D | HIS50 |
D | CYS54 |
D | CYS57 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 109 |
Chain | Residue |
F | HIS25 |
F | HIS50 |
F | CYS54 |
F | CYS57 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN H 109 |
Chain | Residue |
H | HIS25 |
H | HIS50 |
H | CYS54 |
H | CYS57 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN J 109 |
Chain | Residue |
J | HIS25 |
J | HIS50 |
J | CYS54 |
J | CYS57 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN L 110 |
Chain | Residue |
L | HIS25 |
L | HIS50 |
L | CYS54 |
L | CYS57 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN N 109 |
Chain | Residue |
N | HIS25 |
N | HIS50 |
N | CYS54 |
N | CYS57 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN P 110 |
Chain | Residue |
P | HIS25 |
P | HIS50 |
P | CYS54 |
P | CYS57 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN R 109 |
Chain | Residue |
R | HIS25 |
R | HIS50 |
R | CYS54 |
R | CYS57 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN T 109 |
Chain | Residue |
T | HIS25 |
T | HIS50 |
T | CYS54 |
T | CYS57 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20184899 |
Chain | Residue | Details |
B | HIS25 | |
F | HIS50 | |
F | CYS54 | |
F | CYS57 | |
H | HIS25 | |
H | HIS50 | |
H | CYS54 | |
H | CYS57 | |
J | HIS25 | |
J | HIS50 | |
J | CYS54 | |
B | HIS50 | |
J | CYS57 | |
L | HIS25 | |
L | HIS50 | |
L | CYS54 | |
L | CYS57 | |
N | HIS25 | |
N | HIS50 | |
N | CYS54 | |
N | CYS57 | |
P | HIS25 | |
B | CYS54 | |
P | HIS50 | |
P | CYS54 | |
P | CYS57 | |
R | HIS25 | |
R | HIS50 | |
R | CYS54 | |
R | CYS57 | |
T | HIS25 | |
T | HIS50 | |
T | CYS54 | |
B | CYS57 | |
T | CYS57 | |
D | HIS25 | |
D | HIS50 | |
D | CYS54 | |
D | CYS57 | |
F | HIS25 |