Research workbench
Crystal structure of FSA2
Analyse Crystal structure of FSA2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E5T
- Type
- protein
- Length
- 2,980 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diels-alderase FSA2
- EC
- 5.5.1.-
- UniProt
- A0A0E4AYE7
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 5 distinct chains · 3% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, G, H | Diels-alderase FSA2 (EC 5.5.1.-) | protein | 374 | 3% helix, 55% strand | A0A0E4AYE7 |
| B | Diels-alderase FSA2 (EC 5.5.1.-) | protein | 370 | 3% helix, 55% strand | A0A0E4AYE7 |
| C | Diels-alderase FSA2 (EC 5.5.1.-) | protein | 373 | 2% helix, 54% strand | A0A0E4AYE7 |
| D | Diels-alderase FSA2 (EC 5.5.1.-) | protein | 369 | 3% helix, 54% strand | A0A0E4AYE7 |
| E | Diels-alderase FSA2 (EC 5.5.1.-) | protein | 372 | 3% helix, 56% strand | A0A0E4AYE7 |
Ligands and binding sites
- EOH · Ethanol · additive · 8 copies · chains B, H, C, D, A, E
- PGE · Triethylene glycol · additive · chains A, F
- 1PE · Pentaethylene glycol · additive · chains H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1051 | 0.87 | 0.88 | 119 | empty |
| 2 | 715 | 0.84 | 0.88 | 106 | EOH |
| 3 | 454 | 0.80 | 0.87 | 45 | empty |
| 4 | 692 | 0.80 | 0.84 | 90 | empty |
| 5 | 485 | 0.79 | 0.86 | 50 | empty |
Interfaces
15 interfaces between chains.
- B–H · 1030 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 960 Ų buried · 19 hydrogen bonds · protein-protein
- B–E · 951 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 793 Ų buried · 14 hydrogen bonds · protein-protein
- A–G · 753 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7E5T · Crystal structure of Fsa2 · 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 A0A0E4AYE7
- Elsewhere: RCSB PDB 7E5T · PDBe 7E5T · UniProt A0A0E4AYE7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.