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Crystal structure of ipgc in complex with J52
Analyse Crystal structure of ipgc in complex with J52 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PE0
- Type
- protein
- Length
- 270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein ipgc
- UniProt
- P0A2U4
- Ligands
- 483, MG, CL
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein ipgc | protein | 128 | 76% helix, 0% strand | P0A2U4 |
| B | Chaperone protein ipgc | protein | 142 | 75% helix, 0% strand | P0A2U4 |
Ligands and binding sites
- 483 · 2-(1H-imidazol-1-yl)-N-(trans-4-methylcyclohexyl)acetamide · ligand · chains A, B
- MG · Magnesium ion · metal · chains B
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.60 | 0.85 | 20 | 483 |
| 2 | 231 | 0.59 | 0.80 | 37 | empty |
| 3 | 77 | 0.35 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 878 Ų buried · 7 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 P0A2U4
- Elsewhere: RCSB PDB 7PE0 · PDBe 7PE0 · UniProt P0A2U4
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