Research workbench
Altered dimer interface decreases stability in an amyloidogenic KAPPA1 bence jones protein.
Analyse Altered dimer interface decreases stability in an amyloidogenic KAPPA1 bence… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q1E
- Type
- protein
- Length
- 436 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amyloidogenic immunoglobulin light chain protein al-09
- UniProt
- A2NI60
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Amyloidogenic immunoglobulin light chain protein al-09 | protein | 109 | 3% helix, 49% strand | A2NI60 |
Ligands and binding sites
- SO4 · Sulfate ion · ion
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- C–D · 697 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 680 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2Q1E · Altered dimer interface decreases stability in an amyloidogenic kappa1 Bence Jones… · 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 A2NI60
- Elsewhere: RCSB PDB 2Q1E · PDBe 2Q1E · UniProt A2NI60
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