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Crystal structure of pucm in the absence of substrate
Analyse Crystal structure of pucm in the absence of substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H0E
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin-like protein pucm
- UniProt
- O32142
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transthyretin-like protein pucm | protein | 112 | 8% helix, 41% strand | O32142 |
| B | Transthyretin-like protein pucm | protein | 114 | 9% helix, 41% strand | O32142 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.48 | 0.76 | 19 | empty |
| 2 | 61 | 0.35 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 449 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
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 O32142
- Elsewhere: RCSB PDB 2H0E · PDBe 2H0E · UniProt O32142
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