Research workbench
Hhip-C in complex with heparin
Analyse Hhip-C in complex with heparin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PGM
- Type
- protein
- Length
- 1,303 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hedgehog-interacting protein
- UniProt
- Q96QV1
- Ligands
- SGN, IDS
- Pockets
- 14 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 5% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hedgehog-interacting protein | protein | 447 | 5% helix, 39% strand | Q96QV1 |
| B | Hedgehog-interacting protein | protein | 427 | 5% helix, 40% strand | Q96QV1 |
| C | Hedgehog-interacting protein | protein | 429 | 5% helix, 41% strand | Q96QV1 |
Ligands and binding sites
- SGN · 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · sugar · 4 copies · chains B
- IDS · 2-O-sulfo-alpha-L-idopyranuronic acid · sugar · 4 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1077 | 0.81 | 0.82 | 90 | empty |
| 2 | 925 | 0.80 | 0.82 | 80 | empty |
| 3 | 971 | 0.80 | 0.82 | 87 | empty |
| 4 | 534 | 0.72 | 0.80 | 69 | empty |
| 5 | 250 | 0.69 | 0.85 | 42 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1107 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 714 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 248 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 33 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 7PGM · PDBe 7PGM · UniProt Q96QV1
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