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The 2.1 a structure of a tumour suppressing serpin
Analyse The 2.1 a structure of a tumour suppressing serpin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WZ9
- Type
- protein
- Length
- 724 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maspin precursor
- UniProt
- P36952
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maspin precursor | protein | 363 | 33% helix, 33% strand | P36952 |
| B | Maspin precursor | protein | 361 | 33% helix, 33% strand | P36952 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.70 | 0.94 | 24 | empty |
| 2 | 333 | 0.60 | 0.77 | 42 | SO4 |
| 3 | 93 | 0.51 | 0.83 | 16 | empty |
| 4 | 98 | 0.38 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 626 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (artifact).
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 P36952
- Elsewhere: RCSB PDB 1WZ9 · PDBe 1WZ9 · UniProt P36952
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