Research workbench
Crystal structure of lrr domain from shigella flexneri IPAH1.4
Analyse Crystal structure of lrr domain from shigella flexneri IPAH1.4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V8H
- Type
- protein
- Length
- 472 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ring-type E3 ubiquitin transferase
- EC
- 2.3.2.27
- UniProt
- Q9AFJ5
- Pockets
- 4 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ring-type E3 ubiquitin transferase (EC 2.3.2.27) | protein | 236 | 17% helix, 13% strand | Q9AFJ5 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.43 | 0.79 | 21 | empty |
| 2 | 55 | 0.40 | 0.81 | 16 | empty |
| 3 | 101 | 0.35 | 0.74 | 27 | empty |
| 4 | 95 | 0.32 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 956 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7V8H · Crystal structure of LRR domain from Shigella flexneri IpaH1.4 · the same entry in another collection · chain B against B, 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 Q9AFJ5
- Elsewhere: RCSB PDB 7V8H · PDBe 7V8H · UniProt Q9AFJ5
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