Research workbench
Crystal structure of human NFAT1 and fos-jun on the il-2 ARRE1 site
Analyse Crystal structure of human NFAT1 and fos-jun on the il-2 ARRE1 site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S9K
- Type
- protein + DNA
- Length
- 425 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human il-2 ARRE1 promoter element, plus strand; Human il-2 ARRE1 promoter element, minus…
- UniProt
- Q13469, P01100, P05412
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 5 distinct chains · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human il-2 ARRE1 promoter element, plus strand | dna | 20 | — | — |
| B | Human il-2 ARRE1 promoter element, minus strand | dna | 20 | — | — |
| C | Nuclear factor of activated T-cells, cytoplasmic 2 | protein | 280 | 5% helix, 41% strand | Q13469 |
| D | Proto-oncogene protein C-fos | protein | 53 | 92% helix, 0% strand | P01100 |
| E | Transcription factor ap-1 | protein | 52 | 90% helix, 0% strand | P05412 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 878 | 0.81 | 0.83 | 74 | empty |
| 2 | 188 | 0.57 | 0.81 | 29 | empty |
| 3 | 157 | 0.53 | 0.80 | 21 | empty |
| 4 | 108 | 0.51 | 0.82 | 22 | empty |
| 5 | 119 | 0.50 | 0.81 | 15 | empty |
Interfaces
10 interfaces between chains.
- D–E · 1018 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 821 Ų buried · 61 hydrogen bonds · nucleic-nucleic
- B–C · 595 Ų buried · 15 hydrogen bonds · protein-nucleic
- C–D · 439 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 416 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 1S9K · Crystal Structure of Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site · the same entry in another collection · chain E against E, TM-score 1.00
- P01100 · AlphaFold monomer V2.0 prediction for proto-oncogene C-fos (P01100) · a predicted model of the same protein · chain D against A, TM-score 0.89
- P05412 · AlphaFold monomer V2.0 prediction for transcription factor ap-1 (P05412) · a predicted model of the same protein · chain E against A, TM-score 0.65
- Q13469 · AlphaFold monomer V2.0 prediction for nuclear factor of activated T-cells, cytoplasmic 2… · a predicted model of the same protein · chain C against A, TM-score 0.64
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
- Every structure of UniProt P01100
- Every structure of UniProt P05412
- Elsewhere: RCSB PDB 1S9K · PDBe 1S9K · UniProt Q13469 · UniProt P01100 · UniProt P05412
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