Research workbench
M4L/Y(27D)D/T94H mutant of len
Analyse M4L/Y(27D)D/T94H mutant of len in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EEQ
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kappa-4 immunoglobulin (light chain)
- UniProt
- P01625
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Kappa-4 immunoglobulin (light chain) | protein | 113 | 3% helix, 51% strand | P01625 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.60 | 0.81 | 21 | empty |
| 2 | 102 | 0.35 | 0.73 | 22 | empty |
| 3 | 77 | 0.32 | 0.74 | 28 | empty |
| 4 | 60 | 0.27 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 710 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1EEQ · M4L/Y(27D)D/T94H Mutant of LEN · 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 P01625
- Elsewhere: RCSB PDB 1EEQ · PDBe 1EEQ · UniProt P01625
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