Research workbench
NMR structure of DFF40 and DFF45 N-terminal domain complex
Analyse NMR structure of DFF40 and DFF45 N-terminal domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IBX
- Type
- protein
- Length
- 170 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA fragmentation factor 40; Chimera of IgG binding protein G and DNA fragmentation…
- EC
- 3.-.-.-
- UniProt
- O76075, P19909
- Pockets
- 2 · best druggability 0.63
Structure
solution nmr · 2 distinct chains · 17% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA fragmentation factor 40 (EC 3.-.-.-) | protein | 81 | 14% helix, 16% strand | O76075 |
| B | Chimera of IgG binding protein G and DNA fragmentation factor 45 | protein | 89 | 20% helix, 15% strand | P19909 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.63 | 0.89 | 24 | empty |
| 2 | 104 | 0.39 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 669 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1IBX · NMR structure of DFF40 and DFF45 N-terminal domain complex · the same entry in another collection · chain A against A, TM-score 1.00
- O76075 · AlphaFold monomer V2.0 prediction for DNA fragmentation factor subunit beta (O76075) · a predicted model of the same protein · chain A against A, TM-score 0.62
- P19909 · AlphaFold monomer V2.0 prediction for immunoglobulin G-binding protein G (P19909) · a predicted model of the same protein · chain B against A, TM-score 0.45
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 O76075
- Every structure of UniProt P19909
- Elsewhere: RCSB PDB 1IBX · PDBe 1IBX · UniProt O76075 · UniProt P19909
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