MolNFT v1 · #36066 · protein
Structure and mechanism of menf, the menaquinone-specific isochorismate synthase from escherichia COLI
2EUA: “Structure and mechanism of menf, the menaquinone-specific isochorismate synthase from escherichia COLI”. X-ray diffraction, 7 pockets (best druggability 0.73). MolNFT v1 #36066 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2EUA
- Type
- protein
- Length
- 856 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Menaquinone-specific isochorismate synthase
- EC
- 5.4.4.2
- UniProt
- P38051
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Menaquinone-specific isochorismate synthase (EC 5.4.4.2) | protein | 428 | 31% helix, 35% strand | P38051 |
Ligands and binding sites
- TAR · D(-)-tartaric acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 462 | 0.73 | 0.82 | 49 | empty |
| 2 | 442 | 0.73 | 0.83 | 41 | empty |
| 3 | 534 | 0.66 | 0.77 | 71 | empty |
| 4 | 157 | 0.50 | 0.78 | 27 | empty |
| 5 | 71 | 0.39 | 0.79 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 685 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2EUA · Structure and Mechanism of MenF, the Menaqui -Specific Isochorismate Synthase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P38051 · AlphaFold monomer V2.0 prediction for isochorismate synthase menf (P38051) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P38051
- Elsewhere: RCSB PDB 2EUA · PDBe 2EUA · UniProt P38051
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.