Research workbench
NMR structure of the phyrsl-nepr complex from sphingomonas sp. FR1
Analyse NMR structure of the phyrsl-nepr complex from sphingomonas sp. FR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LFW
- Type
- protein
- Length
- 219 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phyr sigma-like domain; Nepr anti sigma factor
- Pockets
- 3 · best druggability 0.75
Structure
solution nmr · 2 distinct chains · 38% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phyr sigma-like domain | protein | 157 | 45% helix, 0% strand | — |
| B | Nepr anti sigma factor | protein | 62 | 21% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.75 | 0.90 | 36 | empty |
| 2 | 78 | 0.45 | 0.81 | 19 | empty |
| 3 | 65 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1334 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2LFW · NMR structure of the PhyRSL-NepR complex from Sphingomonas sp. Fr1 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 2LFW · PDBe 2LFW
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