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Crystal structure of sialostatin L
Analyse Crystal structure of sialostatin L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZM8
- Type
- protein
- Length
- 436 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative secreted cystatin
- UniProt
- Q8MVB6
- Pockets
- 1 · best druggability 0.26
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Putative secreted cystatin | protein | 109 | 15% helix, 46% strand | Q8MVB6 |
| D | Putative secreted cystatin | protein | 109 | 14% helix, 47% strand | Q8MVB6 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.26 | 0.73 | 14 | empty |
Interfaces
4 interfaces between chains.
- C–D · 3325 Ų buried · 67 hydrogen bonds · protein-protein
- A–B · 3279 Ų buried · 67 hydrogen bonds · protein-protein
- A–C · 210 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 17 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 Q8MVB6
- Elsewhere: RCSB PDB 4ZM8 · PDBe 4ZM8 · UniProt Q8MVB6
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