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
- 1FVH
- Type
- protein
- Length
- 546 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SEC1
- UniProt
- O62547
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SEC1 | protein | 546 | 45% helix, 14% strand | O62547 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.61 | 0.78 | 40 | empty |
| 2 | 275 | 0.57 | 0.78 | 38 | empty |
| 3 | 88 | 0.35 | 0.75 | 17 | empty |
Compared structures
- 1FVH · 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 1FVH · PDBe 1FVH · UniProt O62547
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