MolNFT v1 · #29404 · protein
Crystal structure of fragment of mouse ubiquitin-activating enzyme
1Z7L · Ubiquitin-activating enzyme E1 1: “Crystal structure of fragment of mouse ubiquitin-activating enzyme”. X-ray diffraction, 1 ligand (TBR), 12 pockets (best druggability 0.77). MolNFT v1 #29404 on GenesisL1: 3D structure, binding…
- PDB
- 1Z7L
- Type
- protein
- Length
- 765 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-activating enzyme E1 1
- UniProt
- Q02053
- Ligands
- TBR
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Ubiquitin-activating enzyme E1 1 | protein | 255 | 54% helix, 1% strand | Q02053 |
Ligands and binding sites
- TBR · Hexatantalum dodecabromide · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 594 | 0.77 | 0.83 | 67 | empty |
| 2 | 279 | 0.67 | 0.83 | 40 | empty |
| 3 | 375 | 0.59 | 0.76 | 47 | empty |
| 4 | 180 | 0.52 | 0.78 | 23 | empty |
| 5 | 172 | 0.51 | 0.78 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 640 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 615 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 606 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1Z7L · Crystal structure of fragment of mouse ubiquitin-activating enzyme · the same entry in another collection · chain A against A, TM-score 1.00
- Q02053 · AlphaFold monomer V2.0 prediction for ubiquitin-like modifier- activating enzyme 1… · a predicted model of the same protein · chain A 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 Q02053
- Elsewhere: RCSB PDB 1Z7L · PDBe 1Z7L · UniProt Q02053
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