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Crystal structure of nhl domain of TRIM71
Analyse Crystal structure of nhl domain of TRIM71 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QRX
- Type
- protein
- Length
- 558 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase TRIM71
- EC
- 2.3.2.27
- UniProt
- Q2Q1W2
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | E3 ubiquitin-protein ligase TRIM71 (EC 2.3.2.27) | protein | 279 | 8% helix, 47% strand | Q2Q1W2 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 18 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.67 | 0.81 | 39 | EDO |
| 2 | 374 | 0.67 | 0.81 | 36 | EDO |
| 3 | 142 | 0.41 | 0.74 | 20 | EDO |
| 4 | 134 | 0.37 | 0.73 | 25 | EDO |
| 5 | 53 | 0.29 | 0.75 | 13 | EDO |
Interfaces
1 interface between chains.
- A–B · 331 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 Q2Q1W2
- Elsewhere: RCSB PDB 7QRX · PDBe 7QRX · UniProt Q2Q1W2
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