Research workbench
LEF1 hmg domain (from mouse), complexed with DNA (15BP), NMR, 12 structures
Analyse LEF1 hmg domain (from mouse), complexed with DNA (15BP), NMR, 12 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LEF
- Type
- protein + DNA
- Length
- 116 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(*CP*AP*CP*CP*CP*TP*TP*TP*GP*AP*AP*GP*CP*TP*C)- 3'); DNA…
- UniProt
- P27782
- Pockets
- 2 · best druggability 0.40
Structure
solution nmr · 3 distinct chains · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | DNA (5'-D(*CP*AP*CP*CP*CP*TP*TP*TP*GP*AP*AP*GP*CP*TP*C)- 3') | dna | 15 | — | — |
| C | DNA (5'-D(*GP*AP*GP*CP*TP*TP*CP*AP*AP*AP*GP*GP*GP*TP*G)- 3') | dna | 15 | — | — |
| A | Protein (lymphoid enhancer-binding factor) | protein | 86 | 57% helix, 0% strand | P27782 |
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 | 71 | 0.40 | 0.80 | 13 | empty |
| 2 | 91 | 0.38 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- C–A · 1081 Ų buried · 27 hydrogen bonds · protein-nucleic
- B–A · 1051 Ų buried · 23 hydrogen bonds · protein-nucleic
- B–C · 659 Ų buried · 79 hydrogen bonds · nucleic-nucleic
Compared structures
- 2LEF · LEF1 hmg domain (from mouse), complexed with DNA (15BP), NMR, 12 structures · the same entry in another collection · chain B against B, TM-score 1.00
- P27782 · AlphaFold monomer V2.0 prediction for lymphoid enhancer-binding factor 1 (P27782) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 P27782
- Elsewhere: RCSB PDB 2LEF · PDBe 2LEF · UniProt P27782
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