Research workbench
Self-assembly of spider silk proteins is controlled by a pH-sensitive relay
Analyse Self-assembly of spider silk proteins is controlled by a pH-sensitive relay in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LRD
- Type
- protein
- Length
- 255 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major ampullate spidroin 1
- UniProt
- Q05H60
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major ampullate spidroin 1 | protein | 129 | 74% helix, 0% strand | Q05H60 |
| B | Major ampullate spidroin 1 | protein | 126 | 75% helix, 0% strand | Q05H60 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
- PGE · Triethylene glycol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1499 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3LRD · Self-assembly of spider silk proteins is controlled by a pH-sensitive relay · 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 Q05H60
- Elsewhere: RCSB PDB 3LRD · PDBe 3LRD · UniProt Q05H60
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.