Research workbench
Ethylene forming enzyme apo form
Analyse Ethylene forming enzyme apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V2U
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming enzyme
- EC
- 1.13.12.19, 1.14.11.34
- UniProt
- P32021
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-oxoglutarate-dependent ETHYLENE/SUCCINATE-forming enzyme (EC 1.13.12.19, 1.14.11.34) | protein | 344 | 33% helix, 17% strand | P32021 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 476 | 0.70 | 0.80 | 50 | empty |
| 2 | 128 | 0.42 | 0.76 | 19 | empty |
| 3 | 61 | 0.34 | 0.77 | 17 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
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 P32021
- Elsewhere: RCSB PDB 5V2U · PDBe 5V2U · UniProt P32021
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