Research workbench
Crystal structure of FOXC2-dbd bound to a palindromic DNA sequence
Analyse Crystal structure of FOXC2-dbd bound to a palindromic DNA sequence in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LBM
- Type
- protein + DNA
- Length
- 124 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Forkhead box protein C2; IRE0
- UniProt
- Q99958
- Ligands
- MG
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 3 distinct chains · 45% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Forkhead box protein C2 | protein | 95 | 45% helix, 9% strand | Q99958 |
| A | IRE0 | dna | 15 | — | — |
| B | IRE0 | dna | 14 | — | — |
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
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.40 | 0.75 | 15 | empty |
| 2 | 53 | 0.36 | 0.80 | 14 | empty |
| 3 | 102 | 0.34 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 628 Ų buried · 52 hydrogen bonds · nucleic-nucleic
- C–B · 437 Ų buried · 7 hydrogen bonds · protein-nucleic
- C–A · 398 Ų buried · 8 hydrogen bonds · protein-nucleic
Compared structures
- 6LBM · Crystal Structure of FOXC2-DBD bound to a palindromic DNA sequence · 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 0.89
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 6LBM · PDBe 6LBM · UniProt Q99958
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