Research workbench
Structure of the human nuclear cap-binding-complex (cbc)
Analyse Structure of the human nuclear cap-binding-complex (cbc) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H2V
- Type
- protein
- Length
- 815 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 80 kda nuclear cap binding protein; 20 kda nuclear cap binding protein
- UniProt
- Q09161, P52298
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | 80 kda nuclear cap binding protein | protein | 722 | 68% helix, 1% strand | Q09161 |
| Z | 20 kda nuclear cap binding protein | protein | 93 | 23% helix, 33% strand | P52298 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 762 | 0.79 | 0.83 | 61 | empty |
| 2 | 480 | 0.74 | 0.83 | 52 | empty |
| 3 | 232 | 0.62 | 0.81 | 32 | empty |
| 4 | 419 | 0.62 | 0.77 | 58 | empty |
| 5 | 147 | 0.42 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- C–Z · 1303 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 1H2V · Structure of the human nuclear cap-binding-complex (CBC) · the same entry in another collection · chain C against C, TM-score 1.00
- Q09161 · AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (Q09161) · a predicted model of the same protein · chain C against A, TM-score 1.00
- P52298 · AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2 (P52298) · a predicted model of the same protein · chain Z against A, TM-score 0.98
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 Q09161
- Every structure of UniProt P52298
- Elsewhere: RCSB PDB 1H2V · PDBe 1H2V · UniProt Q09161 · UniProt P52298
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