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Structure of VP14 in complex with oxygen
Analyse Structure of VP14 in complex with oxygen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NPE
- Type
- protein
- Length
- 522 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 9-cis-epoxycarotenoid dioxygenase 1, chloroplastic
- EC
- 1.13.11.51
- UniProt
- O24592
- Ligands
- FE2, OXY, OH
- Pockets
- 2 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 9-cis-epoxycarotenoid dioxygenase 1, chloroplastic (EC 1.13.11.51) | protein | 522 | 14% helix, 35% strand | O24592 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · chains A
- OXY · Oxygen molecule · ion · chains A
- OH · Hydroxide ion · ion · chains A
- DIO · 1,4-diethylene dioxide · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 970 | 0.84 | 0.85 | 106 | OXY, OH |
| 2 | 386 | 0.79 | 0.89 | 42 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 O24592
- Elsewhere: RCSB PDB 3NPE · PDBe 3NPE · UniProt O24592
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