Research workbench
Structure of the mouse SORCS2-ngf complex
Analyse Structure of the mouse SORCS2-ngf complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FFY
- Type
- protein
- Length
- 1,139 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9EPR5, P01139
- Ligands
- NAG, BMA
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 918 | — | Q9EPR5 |
| B | — | protein | 110 | — | P01139 |
| C | — | protein | 111 | — | P01139 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FFY · Structure of the mouse SorCS2-NGF complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9EPR5 · AlphaFold monomer V2.0 prediction for VPS10 domain-containing receptor SORCS2 (Q9EPR5) · a predicted model of the same protein · chain A against A, TM-score 0.92
- P01139 · AlphaFold monomer V2.0 prediction for beta-nerve growth factor (P01139) · a predicted model of the same protein · chain C against A, TM-score 0.91
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 Q9EPR5
- Every structure of UniProt P01139
- Elsewhere: RCSB PDB 6FFY · PDBe 6FFY · UniProt Q9EPR5 · UniProt P01139
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