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The human slit 2 dimerization domain D4
Analyse The human slit 2 dimerization domain D4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WFH
- Type
- protein
- Length
- 362 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Slit homolog 2 protein C-product
- UniProt
- O94813
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Slit homolog 2 protein C-product | protein | 181 | 13% helix, 17% strand | O94813 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.35 | 0.76 | 13 | empty |
| 2 | 67 | 0.32 | 0.75 | 15 | empty |
| 3 | 60 | 0.31 | 0.76 | 20 | empty |
| 4 | 53 | 0.27 | 0.74 | 13 | empty |
| 5 | 51 | 0.26 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1313 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 O94813
- Elsewhere: RCSB PDB 2WFH · PDBe 2WFH · UniProt O94813
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