Research workbench
Structure basis of allosteric inhibition of BACE1 by an exosite- binding antibody
Analyse Structure basis of allosteric inhibition of BACE1 by an exosite- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R1G
- Type
- protein
- Length
- 812 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P56817
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 381 | — | P56817 |
| H | — | protein | 217 | — | — |
| L | — | protein | 214 | — | — |
Compared structures
- 3R1G · Structure Basis of Allosteric Inhibition of BACE1 by an Exosite-Binding Antibody · the same entry in another collection · chain B against B, TM-score 1.00
- P56817 · AlphaFold monomer V2.0 prediction for beta-secretase 1 (P56817) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P56817
- Elsewhere: RCSB PDB 3R1G · PDBe 3R1G · UniProt P56817
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