Research workbench
Ptprg CNTN4 complex
Analyse Ptprg CNTN4 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KLD
- Type
- protein
- Length
- 638 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Contactin 4; Receptor-type tyrosine-protein phosphatase gamma
- EC
- 3.1.3.48
- UniProt
- Q14BL8, Q05909
- Ligands
- NAG
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Contactin 4 | protein | 376 | 3% helix, 58% strand | Q14BL8 |
| B | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 262 | 16% helix, 32% strand | Q05909 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 219 | 0.52 | 0.76 | 27 | empty |
| 2 | 136 | 0.49 | 0.79 | 30 | empty |
| 3 | 78 | 0.36 | 0.77 | 13 | empty |
| 4 | 61 | 0.27 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 927 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
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 Q14BL8
- Every structure of UniProt Q05909
- Elsewhere: RCSB PDB 3KLD · PDBe 3KLD · UniProt Q14BL8 · UniProt Q05909
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