MolNFT v1 · #76562 · protein
Domain-domain flexibility leads to allostery within the camp receptor protein (crp)
3QOP: “Domain-domain flexibility leads to allostery within the camp receptor protein (crp)”. X-ray diffraction. MolNFT v1 #76562 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3QOP
- Type
- protein
- Length
- 400 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0ACJ8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 200 | — | P0ACJ8 |
Compared structures
- 3QOP · Domain-domain flexibility leads to allostery within the camp receptor protein (CRP) · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACJ8 · AlphaFold monomer V2.0 prediction for camp-activated global transcriptional regulator crp… · 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 P0ACJ8
- Elsewhere: RCSB PDB 3QOP · PDBe 3QOP · UniProt P0ACJ8
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