MolNFT v1 · #27967 · protein
Fusarium solani cutinase complex with DI(ISOPROPYL)PHOSPHATE
1XZK: “Fusarium solani cutinase complex with DI(ISOPROPYL)PHOSPHATE”. X-ray diffraction, 1 ligand (DFP), 1 pocket (best druggability 0.68). MolNFT v1 #27967 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1XZK
- Type
- protein
- Length
- 394 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase
- EC
- 3.1.1.-
- UniProt
- P00590
- Ligands
- DFP
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cutinase (EC 3.1.1.-) | protein | 197 | 45% helix, 16% strand | P00590 |
Ligands and binding sites
- DFP · Diisopropyl phosphonate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 446 | 0.68 | 0.79 | 51 | DFP |
Interfaces
1 interface between chains.
- A–B · 187 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 2 covalent (disulfide, covalent ligand).
Compared structures
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 P00590
- Elsewhere: RCSB PDB 1XZK · PDBe 1XZK · UniProt P00590
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.