Research workbench
Structure of a human bence-jones dimer crystallized in U.S. space shuttle mission sts-95: 100K
Analyse Structure of a human bence-jones dimer crystallized in U.S. space shuttle… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LGV
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin lambda light chain
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Immunoglobulin lambda light chain | protein | 214 | 6% helix, 50% strand | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.65 | 0.81 | 37 | empty |
| 2 | 364 | 0.54 | 0.74 | 41 | empty |
| 3 | 180 | 0.44 | 0.74 | 33 | empty |
| 4 | 62 | 0.31 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1675 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 2 modified (disulfide, cyclization).
Compared structures
- 1LGV · Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95… · 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
- Elsewhere: RCSB PDB 1LGV · PDBe 1LGV
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