Research workbench
Crystal structures of the lsrr proteins complexed with phospho-ai-2 and its two different analogs reveal distinct mechanisms for ligand recognition
Analyse Crystal structures of the lsrr proteins complexed with phospho-ai-2 and its two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L4Y
- Type
- protein
- Length
- 477 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator lsrr
- UniProt
- P76141
- Pockets
- 6 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator lsrr | protein | 237 | 45% helix, 17% strand | P76141 |
| B | Transcriptional regulator lsrr | protein | 240 | 45% helix, 18% strand | P76141 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.50 | 0.84 | 21 | empty |
| 2 | 135 | 0.43 | 0.75 | 32 | empty |
| 3 | 88 | 0.34 | 0.75 | 20 | empty |
| 4 | 60 | 0.30 | 0.74 | 11 | empty |
| 5 | 77 | 0.29 | 0.72 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 749 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4L4Y · Crystal structures of the LsrR proteins complexed with phospho-AI-2 and its two different… · the same entry in another collection · chain B against B, TM-score 1.00
- P76141 · AlphaFold monomer V2.0 prediction for transcriptional regulator lsrr (P76141) · 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 P76141
- Elsewhere: RCSB PDB 4L4Y · PDBe 4L4Y · UniProt P76141
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