MolNFT v1 · #107336 · protein
The carboxy-terminal domain of ERB1 is a seven-bladed beta-propeller that binds RNA.
4U7A · Ribosome biogenesis protein ERB1: “The carboxy-terminal domain of ERB1 is a seven-bladed beta-propeller that binds RNA.”. X-ray diffraction, 2 pockets (best druggability 0.78). MolNFT v1 #107336 on GenesisL1: 3D structure, binding…
- PDB
- 4U7A
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosome biogenesis protein ERB1
- UniProt
- Q04660
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosome biogenesis protein ERB1 | protein | 356 | 8% helix, 46% strand | Q04660 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- GOL · Glycerol · additive · chains A
- EOH · Ethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.78 | 0.84 | 54 | empty |
| 2 | 55 | 0.30 | 0.75 | 17 | EOH |
Compared structures
- 4U7A · The carboxy-terminal domain of Erb1 is a seven-bladed beta-propeller that binds RNA. · the same entry in another collection · chain A against A, TM-score 1.00
- Q04660 · AlphaFold monomer V2.0 prediction for ribosome biogenesis protein ERB1 (Q04660) · a predicted model of the same protein · 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 Q04660
- Elsewhere: RCSB PDB 4U7A · PDBe 4U7A · UniProt Q04660
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