Research workbench
Structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa with bound salicylate and pyruvate
Analyse Structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3REM
- Type
- protein
- Length
- 194 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Salicylate biosynthesis protein pchb
- EC
- 4.1.99.-
- UniProt
- Q51507
- Ligands
- SAL, PYR
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Salicylate biosynthesis protein pchb (EC 4.1.99.-) | protein | 97 | 79% helix, 0% strand | Q51507 |
Ligands and binding sites
- SAL · 2-hydroxybenzoic acid · ligand · 2 copies · chains A, B
- PYR · Pyruvic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.78 | 0.98 | 18 | SAL, PYR |
| 2 | 92 | 0.76 | 0.97 | 18 | PYR, SAL |
Interfaces
1 interface between chains.
- A–B · 2501 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3REM · Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aerugionsa with Bound… · the same entry in another collection · chain A against A, TM-score 1.00
- Q51507 · AlphaFold monomer V2.0 prediction for isochorismate pyruvate lyase (Q51507) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q51507
- Elsewhere: RCSB PDB 3REM · PDBe 3REM · UniProt Q51507
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