Research workbench
Crystal structure of a threonine-selective rcr E3 ligase
Analyse Crystal structure of a threonine-selective rcr E3 ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O6C
- Type
- protein
- Length
- 252 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase MYCBP2
- EC
- 2.3.2.27
- UniProt
- O75592
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.27) | protein | 252 | 32% helix, 17% strand | O75592 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.38 | 0.75 | 25 | empty |
| 2 | 70 | 0.34 | 0.76 | 14 | empty |
| 3 | 59 | 0.30 | 0.75 | 17 | empty |
Compared structures
- 5O6C · Crystal Structure of a threonine-selective RCR E3 ligase · the same entry in another collection · 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 O75592
- Elsewhere: RCSB PDB 5O6C · PDBe 5O6C · UniProt O75592
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