MolNFT v1 · #166428 · protein + DNA
Structure of FACT_SUBNUCLEOSOME complex 1
6UPK · Histone H3.1: “Structure of FACT_SUBNUCLEOSOME complex 1”. Electron microscopy, 20 pockets (best druggability 0.80). MolNFT v1 #166428 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UPK
- Type
- protein + DNA
- Length
- 1,512 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3.1; Histone H4; Histone H2A; Histone H2B; Fact complex subunit SPT16; Fact…
- UniProt
- P68431, P62805, Q93077, P62807
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 10 distinct chains · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H3.1 | protein | 76 | 70% helix, 3% strand | P68431 |
| B | Histone H4 | protein | 78 | 67% helix, 3% strand | P62805 |
| C | Histone H2A | protein | 108 | 49% helix, 2% strand | Q93077 |
| D | Histone H2B | protein | 94 | 67% helix, 2% strand | P62807 |
| E | Histone H3.1 | protein | 98 | 66% helix, 3% strand | P68431 |
| F | Histone H4 | protein | 80 | 63% helix, 4% strand | P62805 |
| G | Fact complex subunit SPT16 | protein | 423 | 17% helix, 30% strand | — |
| H | Fact complex subunit SSRP1 | protein | 411 | 11% helix, 37% strand | — |
| I | DNA (79-mer) | dna | 72 | — | — |
| J | DNA (79-mer) | dna | 72 | — | — |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.80 | 0.97 | 29 | empty |
| 2 | 568 | 0.78 | 0.85 | 72 | empty |
| 3 | 254 | 0.78 | 0.90 | 56 | empty |
| 4 | 930 | 0.78 | 0.80 | 123 | empty |
| 5 | 111 | 0.78 | 0.97 | 21 | empty |
Interfaces
35 interfaces between chains.
- I–J · 3365 Ų buried · 341 hydrogen bonds · nucleic-nucleic
- C–D · 2320 Ų buried · 27 hydrogen bonds · protein-protein
- E–F · 2295 Ų buried · 18 hydrogen bonds · protein-protein
- G–H · 2269 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 1766 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 P68431
- Every structure of UniProt P62805
- Every structure of UniProt Q93077
- Every structure of UniProt P62807
- Elsewhere: RCSB PDB 6UPK · PDBe 6UPK · UniProt P68431 · UniProt P62805 · UniProt Q93077 · UniProt P62807
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