2A07
Crystal Structure of Foxp2 bound Specifically to DNA.
Functional Information from GO Data
Chain | GOid | namespace | contents |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0043565 | molecular_function | sequence-specific DNA binding |
G | 0003700 | molecular_function | DNA-binding transcription factor activity |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0043565 | molecular_function | sequence-specific DNA binding |
H | 0003700 | molecular_function | DNA-binding transcription factor activity |
H | 0006355 | biological_process | regulation of DNA-templated transcription |
H | 0043565 | molecular_function | sequence-specific DNA binding |
I | 0003700 | molecular_function | DNA-binding transcription factor activity |
I | 0006355 | biological_process | regulation of DNA-templated transcription |
I | 0043565 | molecular_function | sequence-specific DNA binding |
J | 0003700 | molecular_function | DNA-binding transcription factor activity |
J | 0006355 | biological_process | regulation of DNA-templated transcription |
J | 0043565 | molecular_function | sequence-specific DNA binding |
K | 0003700 | molecular_function | DNA-binding transcription factor activity |
K | 0006355 | biological_process | regulation of DNA-templated transcription |
K | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG F 601 |
Chain | Residue |
F | SER557 |
F | LEU558 |
F | HIS559 |
F | HOH613 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG H 602 |
Chain | Residue |
H | HOH397 |
H | LEU556 |
H | HIS559 |
H | PHE562 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG I 603 |
Chain | Residue |
I | LEU558 |
I | HIS559 |
I | SER557 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG G 604 |
Chain | Residue |
G | LEU556 |
G | HIS559 |
G | PHE562 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG J 605 |
Chain | Residue |
J | LEU556 |
J | SER557 |
J | HIS559 |
J | PHE562 |
J | HOH673 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG K 606 |
Chain | Residue |
D | HOH24 |
K | LEU556 |
K | SER557 |
K | HIS559 |
K | PHE562 |
K | HOH645 |
Functional Information from PROSITE/UniProt
site_id | PS00658 |
Number of Residues | 7 |
Details | FORK_HEAD_2 Fork head domain signature 2. WKNAVRH |
Chain | Residue | Details |
F | TRP548-HIS554 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 540 |
Details | DNA_BIND: Fork-head => ECO:0000255|PROSITE-ProRule:PRU00089 |
Chain | Residue | Details |
F | ARG504-LEU594 | |
G | ARG504-LEU594 | |
H | ARG504-LEU594 | |
I | ARG504-LEU594 | |
J | ARG504-LEU594 | |
K | ARG504-LEU594 |