Research workbench
LRIG1 extracellular domain: structure and function analysis
Analyse LRIG1 extracellular domain: structure and function analysis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U7M
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucine-rich repeats and immunoglobulin-like domains protein 1
- UniProt
- Q96JA1
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucine-rich repeats and immunoglobulin-like domains protein 1 | protein | 289 | 4% helix, 57% strand | Q96JA1 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 4U7M · LRIG1 extracellular domain: Structure and Function Analysis · the same entry in another collection · chain A against A, TM-score 1.00
- Q96JA1 · AlphaFold monomer V2.0 prediction for leucine-rich repeats and immunoglobulin-like… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q96JA1
- Elsewhere: RCSB PDB 4U7M · PDBe 4U7M · UniProt Q96JA1
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