MolNFT v1 · #109497 · protein + DNA
Radiation damage to the nucleoprotein complex C.ESP1396I: dose (dwd) 35.7 mgy
4X4H · Regulatory protein: “Radiation damage to the nucleoprotein complex C.ESP1396I: dose (dwd) 35.7 mgy”. X-ray diffraction, 8 pockets (best druggability 0.52). MolNFT v1 #109497 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4X4H
- Type
- protein + DNA
- Length
- 376 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulatory protein; 35-mer DNA
- UniProt
- Q8GGH0
- Pockets
- 8 · best druggability 0.52
Structure
x-ray diffraction · 4 distinct chains · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Regulatory protein | protein | 76 | 72% helix, 1% strand | Q8GGH0 |
| B, C | Regulatory protein | protein | 77 | 71% helix, 1% strand | Q8GGH0 |
| E | 35-mer DNA | dna | 35 | — | — |
| F | 35-mer DNA | dna | 35 | — | — |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.52 | 0.77 | 22 | empty |
| 2 | 156 | 0.44 | 0.76 | 19 | empty |
| 3 | 68 | 0.37 | 0.78 | 13 | empty |
| 4 | 106 | 0.36 | 0.74 | 16 | empty |
| 5 | 68 | 0.33 | 0.76 | 14 | empty |
Interfaces
12 interfaces between chains.
- E–F · 1589 Ų buried · 124 hydrogen bonds · nucleic-nucleic
- A–B · 999 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 990 Ų buried · 10 hydrogen bonds · protein-protein
- B–F · 443 Ų buried · 8 hydrogen bonds · protein-nucleic
- C–E · 429 Ų buried · 7 hydrogen bonds · protein-nucleic
Compared structures
- 4X4H · RADIATION DAMAGE TO THE NUCLEOPROTEIN COMPLEX C.Esp1396I: DOSE (DWD) 35.7 MGy · the same entry in another collection · chain A against A, 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 Q8GGH0
- Elsewhere: RCSB PDB 4X4H · PDBe 4X4H · UniProt Q8GGH0
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