Research workbench
Structure of NFAT1 bound as a dimer to the HIV-1 ltr kb element
Analyse Structure of NFAT1 bound as a dimer to the HIV-1 ltr kb element in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P7H
- Type
- protein + DNA
- Length
- 1,204 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*AP*AP*TP*GP*GP*GP*GP*AP*CP*TP*TP*TP*CP*CP*A)-3'…
- UniProt
- Q13469
- Pockets
- 15 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 2% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | 5'-D(*AP*AP*TP*GP*GP*GP*GP*AP*CP*TP*TP*TP*CP*CP*A)-3' | dna | 15 | — | — |
| B, D | 5'-D(*TP*TP*TP*GP*GP*AP*AP*AP*GP*TP*CP*CP*CP*CP*A)-3' | dna | 15 | — | — |
| L, M, N, O | Nuclear factor of activated T-cells, cytoplasmic 2 | protein | 286 | 2% helix, 42% strand | Q13469 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1122 | 0.73 | 0.77 | 112 | empty |
| 2 | 613 | 0.68 | 0.77 | 57 | empty |
| 3 | 276 | 0.67 | 0.84 | 31 | empty |
| 4 | 265 | 0.66 | 0.83 | 26 | empty |
| 5 | 246 | 0.64 | 0.83 | 37 | empty |
Interfaces
18 interfaces between chains.
- N–O · 800 Ų buried · 12 hydrogen bonds · protein-protein
- L–M · 798 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 620 Ų buried · 53 hydrogen bonds · nucleic-nucleic
- D–N · 603 Ų buried · 9 hydrogen bonds · protein-nucleic
- A–B · 563 Ų buried · 51 hydrogen bonds · nucleic-nucleic
Compared structures
- 1P7H · Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element · the same entry in another collection · chain O against O, TM-score 1.00
- Q13469 · AlphaFold monomer V2.0 prediction for nuclear factor of activated T-cells, cytoplasmic 2… · a predicted model of the same protein · chain L against A, TM-score 0.66
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 1P7H · PDBe 1P7H · UniProt Q13469
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