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Crystal structure of the human hip ectodomain
Analyse Crystal structure of the human hip ectodomain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WFT
- Type
- protein
- Length
- 846 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hedgehog-interacting protein
- UniProt
- Q96QV1
- Ligands
- NA, CL
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hedgehog-interacting protein | protein | 438 | 5% helix, 41% strand | Q96QV1 |
| B | Hedgehog-interacting protein | protein | 408 | 5% helix, 41% strand | Q96QV1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 865 | 0.80 | 0.82 | 71 | empty |
| 2 | 777 | 0.79 | 0.83 | 61 | empty |
| 3 | 260 | 0.69 | 0.84 | 38 | empty |
| 4 | 233 | 0.68 | 0.85 | 37 | empty |
| 5 | 328 | 0.60 | 0.78 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1097 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 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 Q96QV1
- Elsewhere: RCSB PDB 2WFT · PDBe 2WFT · UniProt Q96QV1
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