Research workbench
The N-terminal domain of beta-B2-crystallin resembles the putative ancestral homodimer
Analyse The N-terminal domain of beta-B2-crystallin resembles the putative ancestral… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E7N
- Type
- protein
- Length
- 178 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-crystallin B2
- UniProt
- P62696
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-crystallin B2 | protein | 89 | 8% helix, 46% strand | P62696 |
Interfaces
1 interface between chains.
- A–B · 860 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1E7N · The N-terminal domain of beta-B2-crystallin resembles the putative ancestral homodimer · the same entry in another collection · chain A against A, TM-score 1.00
- P62696 · AlphaFold monomer V2.0 prediction for beta-crystallin B2 (P62696) · a predicted model of the same protein · chain B 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 P62696
- Elsewhere: RCSB PDB 1E7N · PDBe 1E7N · UniProt P62696
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