Research workbench
Circularly permuted BB2-crystallin
Analyse Circularly permuted BB2-crystallin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BD7
- Type
- protein
- Length
- 347 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Circularly permuted BB2-crystallin
- UniProt
- P62697
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Circularly permuted BB2-crystallin | protein | 176 | 11% helix, 44% strand | P62697 |
| B | Circularly permuted BB2-crystallin | protein | 171 | 10% helix, 48% strand | P62697 |
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 | 111 | 0.55 | 0.84 | 19 | empty |
| 2 | 69 | 0.34 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1477 Ų buried · 23 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 P62697
- Elsewhere: RCSB PDB 1BD7 · PDBe 1BD7 · UniProt P62697
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