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An asymmetric NFAT1-rhr homodimer on a pseudo-palindromic, kappa-B site
Analyse An asymmetric NFAT1-rhr homodimer on a pseudo-palindromic, kappa-B site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PZU
- Type
- protein + DNA
- Length
- 1,740 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*TP*TP*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*A)- 3'…
- UniProt
- Q13469
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 3% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X, V, T | 5'-D(*TP*TP*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*A)- 3' | dna | 14 | — | — |
| Y, Z, W | 5'-D(*AP*AP*TP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*C)- 3' | dna | 14 | — | — |
| B, D, H, I, L, M | Nuclear factor of activated T-cells, cytoplasmic 2 | protein | 276 | 3% helix, 41% strand | Q13469 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1047 | 0.77 | 0.79 | 92 | empty |
| 2 | 828 | 0.76 | 0.80 | 60 | empty |
| 3 | 745 | 0.75 | 0.80 | 59 | empty |
| 4 | 532 | 0.73 | 0.82 | 42 | empty |
| 5 | 700 | 0.71 | 0.78 | 45 | empty |
Interfaces
29 interfaces between chains.
- B–D · 772 Ų buried · 15 hydrogen bonds · protein-protein
- L–M · 763 Ų buried · 14 hydrogen bonds · protein-protein
- H–I · 757 Ų buried · 14 hydrogen bonds · protein-protein
- V–I · 629 Ų buried · 14 hydrogen bonds · protein-nucleic
- X–M · 611 Ų buried · 11 hydrogen bonds · protein-nucleic
Compared structures
- 1PZU · An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site · the same entry in another collection · chain M against M, TM-score 1.00
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 Q13469
- Elsewhere: RCSB PDB 1PZU · PDBe 1PZU · UniProt Q13469
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