Research workbench
Crystal structure of hedgehog bound to the fniii domains of ihog
Analyse Crystal structure of hedgehog bound to the fniii domains of ihog in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IBG
- Type
- protein
- Length
- 1,401 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CG9211-pa; Protein hedgehog
- UniProt
- Q9VM64, Q02936
- Ligands
- PO4
- Pockets
- 19 · best druggability 0.78
Structure
x-ray diffraction · 6 distinct chains · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CG9211-pa | protein | 214 | 1% helix, 43% strand | Q9VM64 |
| B, C, D | CG9211-pa | protein | 213 | 3% helix, 46% strand | Q9VM64 |
| E | Protein hedgehog | protein | 142 | 28% helix, 19% strand | Q02936 |
| F | Protein hedgehog | protein | 132 | 28% helix, 20% strand | Q02936 |
| G | Protein hedgehog | protein | 134 | 25% helix, 23% strand | Q02936 |
| H | Protein hedgehog | protein | 140 | 28% helix, 19% strand | Q02936 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 12 copies · chains A, E, B, C, G, D, H, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1035 | 0.78 | 0.80 | 83 | PO4 |
| 2 | 971 | 0.77 | 0.79 | 77 | PO4 |
| 3 | 94 | 0.45 | 0.79 | 19 | empty |
| 4 | 115 | 0.44 | 0.78 | 25 | empty |
| 5 | 99 | 0.44 | 0.78 | 20 | empty |
Interfaces
11 interfaces between chains.
- B–C · 995 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 933 Ų buried · 10 hydrogen bonds · protein-protein
- A–F · 656 Ų buried · 11 hydrogen bonds · protein-protein
- D–G · 654 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 643 Ų buried · 11 hydrogen bonds · protein-protein
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 Q9VM64
- Every structure of UniProt Q02936
- Elsewhere: RCSB PDB 2IBG · PDBe 2IBG · UniProt Q9VM64 · UniProt Q02936
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