MolNFT v1 · #93398 · protein
Crystal structure of an isochorismatase (PP1826) from pseudomonas putida KT2440 at 1.60 a resolution
4H17 · Hydrolase, isochorismatase family: “Crystal structure of an isochorismatase (PP1826) from pseudomonas putida KT2440 at 1.60 a resolution”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.58). MolNFT v1 #93398 on…
- PDB
- 4H17
- Type
- protein
- Length
- 391 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrolase, isochorismatase family
- UniProt
- Q88LV1
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydrolase, isochorismatase family | protein | 197 | 37% helix, 23% strand | Q88LV1 |
| B | Hydrolase, isochorismatase family | protein | 194 | 37% helix, 23% strand | Q88LV1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.58 | 0.85 | 28 | SO4, EDO |
| 2 | 113 | 0.56 | 0.84 | 26 | SO4 |
| 3 | 156 | 0.43 | 0.75 | 27 | EDO |
| 4 | 138 | 0.42 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1956 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 4H17 · Crystal structure of an isochorismatase (PP1826) from Pseudomonas putida KT2440 at 1.60 A… · 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
- Every structure of UniProt Q88LV1
- Elsewhere: RCSB PDB 4H17 · PDBe 4H17 · UniProt Q88LV1
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