Research workbench
Cryo-EM structure of NCP_THF2(-1)-UV-ddb
Analyse Cryo-EM structure of NCP_THF2(-1)-UV-ddb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R8Z
- Type
- protein + DNA
- Length
- 2,274 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3.1; Histone H4; Histone H2A type 1-B/E; Histone H2B type 1-J; Human…
- UniProt
- P68431, P62805, P04908, P06899, Q16531, Q92466
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 9 distinct chains · 23% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Histone H3.1 | protein | 101 | 62% helix, 4% strand | P68431 |
| B | Histone H4 | protein | 86 | 57% helix, 8% strand | P62805 |
| C, G | Histone H2A type 1-B/E | protein | 117 | 50% helix, 6% strand | P04908 |
| D, H | Histone H2B type 1-J | protein | 97 | 72% helix, 4% strand | P06899 |
| F | Histone H4 | protein | 82 | 60% helix, 9% strand | P62805 |
| I | Human alpha-satellite DNA (145-mer) | dna | 145 | — | — |
| J | Human alpha-satellite DNA (145-mer) with abasic sites at positions 97-98 | dna | 145 | — | — |
| K | DNA damage-binding protein 1 | protein | 825 | 8% helix, 51% strand | Q16531 |
| L | DNA damage-binding protein 2 | protein | 361 | 7% helix, 37% strand | Q92466 |
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 | 773 | 0.82 | 0.86 | 76 | empty |
| 2 | 1139 | 0.80 | 0.81 | 106 | empty |
| 3 | 1018 | 0.78 | 0.80 | 73 | empty |
| 4 | 662 | 0.78 | 0.83 | 73 | empty |
| 5 | 526 | 0.77 | 0.85 | 69 | empty |
Interfaces
41 interfaces between chains.
- I–J · 6172 Ų buried · 411 hydrogen bonds · nucleic-nucleic
- A–B · 2600 Ų buried · 12 hydrogen bonds · protein-protein
- K–L · 2580 Ų buried · 18 hydrogen bonds · protein-protein
- G–H · 2577 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 2573 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nucleotide modification).
Compared structures
- 6R8Z · Cryo-EM structure of NCP_THF2(-1)-UV-DDB · the same entry in another collection · chain L against L, 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 P68431
- Every structure of UniProt P62805
- Every structure of UniProt P04908
- Every structure of UniProt P06899
- Every structure of UniProt Q16531
- Every structure of UniProt Q92466
- Elsewhere: RCSB PDB 6R8Z · PDBe 6R8Z · UniProt P68431 · UniProt P62805 · UniProt P04908 · UniProt P06899 · UniProt Q16531 · UniProt Q92466
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