Research workbench
NMR structure of the third immunoglobulin domain from the neural cell adhesion molecule.
Analyse NMR structure of the third immunoglobulin domain from the neural cell adhesion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IE5
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neural cell adhesion molecule
- UniProt
- P13590
- Pockets
- 1 · best druggability 0.41
Structure
solution nmr · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neural cell adhesion molecule | protein | 107 | 0% helix, 54% strand | P13590 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.41 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1IE5 · NMR structure of the third immunoglobulin domain from the neural cell adhesion molecule. · the same entry in another collection · chain A against A, TM-score 1.00
- P13590 · AlphaFold monomer V2.0 prediction for neural cell adhesion molecule 1 (P13590) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 P13590
- Elsewhere: RCSB PDB 1IE5 · PDBe 1IE5 · UniProt P13590
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