MolNFT v1 · #59353 · protein
Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex
3BVG: “Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex”. X-ray diffraction. MolNFT v1 #59353 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3BVG
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A0L5
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 228 | — | P0A0L5 |
Compared structures
- 3BVG · Manipulating the coupled folding and binding process drives affinity maturation in a… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A0L5 · AlphaFold monomer V2.0 prediction for enterotoxin type C-3 (P0A0L5) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P0A0L5
- Elsewhere: RCSB PDB 3BVG · PDBe 3BVG · UniProt P0A0L5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.