Research workbench
Crystal structure analysis of neuronal SEC1 from the squid L. pealei
Analyse Crystal structure analysis of neuronal SEC1 from the squid L. pealei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FVF
- Type
- protein
- Length
- 1,086 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SEC1
- UniProt
- O62547
- Pockets
- 11 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SEC1 | protein | 543 | 48% helix, 13% strand | O62547 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 358 | 0.64 | 0.79 | 44 | empty |
| 2 | 358 | 0.63 | 0.79 | 42 | empty |
| 3 | 258 | 0.58 | 0.79 | 37 | empty |
| 4 | 263 | 0.57 | 0.78 | 38 | empty |
| 5 | 149 | 0.54 | 0.81 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1417 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1FVF · Crystal structure analysis of neuronal SEC1 from the squid L. pealei · the same entry in another collection · chain A against A, TM-score 1.00
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 O62547
- Elsewhere: RCSB PDB 1FVF · PDBe 1FVF · UniProt O62547
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