Research workbench
Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa
Analyse Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H9C
- Type
- protein
- Length
- 173 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
- NO3
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Salicylate biosynthesis protein pchb (EC 4.1.99.-) | protein | 88 | 80% helix, 0% strand | Q51507 |
| B | Salicylate biosynthesis protein pchb (EC 4.1.99.-) | protein | 85 | 84% helix, 0% strand | Q51507 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 5 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 | 74 | 0.57 | 0.88 | 16 | NO3 |
| 2 | 86 | 0.51 | 0.83 | 17 | NO3 |
Interfaces
1 interface between chains.
- A–B · 2395 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 2H9C · Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa · 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 0.96
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 2H9C · PDBe 2H9C · UniProt Q51507
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