Research workbench
Solid-state NMR structure of the membrane anchor domain of the trimeric autotransporter yada
Analyse Solid-state NMR structure of the membrane anchor domain of the trimeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LME
- Type
- protein
- Length
- 315 residues
- Chains
- 3
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adhesin yada
- UniProt
- A1JUB7
Structure
solid-state nmr · 1 distinct chain · 29% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Adhesin yada | protein | 105 | 29% helix, 41% strand | A1JUB7 |
Interfaces
3 interfaces between chains.
- A–B · 1728 Ų buried · 31 hydrogen bonds · protein-protein
- B–C · 1724 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 1724 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 2LME · Solid-state NMR structure of the membrane anchor domain of the trimeric autotransporter… · the same entry in another collection · chain B against B, TM-score 1.00
- A1JUB7 · AlphaFold monomer V2.0 prediction for adhesin yada (A1JUB7) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 A1JUB7
- Elsewhere: RCSB PDB 2LME · PDBe 2LME · UniProt A1JUB7
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