Research workbench
Cleaved human neuroserpin
Analyse Cleaved human neuroserpin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F02
- Type
- protein
- Length
- 721 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neuroserpin
- UniProt
- Q99574
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neuroserpin | protein | 322 | 33% helix, 38% strand | Q99574 |
| C | Neuroserpin | protein | 35 | 0% helix, 49% strand | Q99574 |
| B | Neuroserpin | protein | 327 | 32% helix, 37% strand | Q99574 |
| D | Neuroserpin | protein | 37 | 0% helix, 46% strand | Q99574 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 669 | 0.68 | 0.77 | 46 | empty |
| 2 | 75 | 0.47 | 0.82 | 19 | empty |
| 3 | 75 | 0.37 | 0.77 | 19 | empty |
| 4 | 59 | 0.37 | 0.78 | 13 | empty |
| 5 | 74 | 0.35 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- B–D · 2489 Ų buried · 41 hydrogen bonds · protein-protein
- A–C · 2482 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 150 Ų buried · 0 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 Q99574
- Elsewhere: RCSB PDB 3F02 · PDBe 3F02 · UniProt Q99574
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