Research workbench
Pseudomonas aeruginosa tola domain III, seleno-methionine derivative
Analyse Pseudomonas aeruginosa tola domain III, seleno-methionine derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LR0
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tola protein
- UniProt
- P50600
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tola protein | protein | 126 | 56% helix, 18% strand | P50600 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 1LR0 · Pseudomonas aeruginosa TolA Domain III, Seleno-methionine Derivative · the same entry in another collection · chain A against A, TM-score 1.00
- P50600 · AlphaFold monomer V2.0 prediction for tol-pal system protein tola (P50600) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P50600
- Elsewhere: RCSB PDB 1LR0 · PDBe 1LR0 · UniProt P50600
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