Research workbench
Crystal structural of FOXC2 DNA binding domain bound to pc promoter
Analyse Crystal structural of FOXC2 DNA binding domain bound to pc promoter in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AKP
- Type
- protein + DNA
- Length
- 126 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(AP*CP*AP*CP*AP*AP*AP*TP*AP*TP*TP*TP*GP*TP*GP*T)- 3'); Forkhead box protein C2
- UniProt
- Q99958
- Ligands
- MG
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA (5'-D(AP*CP*AP*CP*AP*AP*AP*TP*AP*TP*TP*TP*GP*TP*GP*T)- 3') | dna | 16 | — | — |
| C | Forkhead box protein C2 | protein | 94 | 46% helix, 10% strand | Q99958 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.41 | 0.77 | 18 | empty |
| 2 | 73 | 0.28 | 0.73 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 714 Ų buried · 59 hydrogen bonds · nucleic-nucleic
- B–C · 402 Ų buried · 5 hydrogen bonds · protein-nucleic
- A–C · 117 Ų buried · 0 hydrogen bonds · protein-nucleic
Compared structures
- 6AKP · Crystal Structural of FOXC2 DNA binding domain bound to PC promoter · the same entry in another collection · chain C against C, TM-score 1.00
- Q99958 · AlphaFold monomer V2.0 prediction for forkhead box protein C2 (Q99958) · a predicted model of the same protein · chain C against A, TM-score 0.91
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q99958
- Elsewhere: RCSB PDB 6AKP · PDBe 6AKP · UniProt Q99958
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