Research workbench
Crystal structure of the ligand binding domain of E. COLI cynr with its specific effector azide
Analyse Crystal structure of the ligand binding domain of E. COLI cynr with its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HFU
- Type
- protein
- Length
- 811 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P27111
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 202 | — | P27111 |
| B | — | protein | 204 | — | P27111 |
| C | — | protein | 203 | — | P27111 |
Compared structures
- 3HFU · Crystal structure of the ligand binding domain of E. coli CynR with its specific effector… · the same entry in another collection · chain D against D, TM-score 1.00
- P27111 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator cynr (P27111) · a predicted model of the same protein · chain B 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 P27111
- Elsewhere: RCSB PDB 3HFU · PDBe 3HFU · UniProt P27111
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