Research workbench
Chloroperoxidase from the fungus curvularia inaequalis: recombinant holo-chloroperoxidase
Analyse Chloroperoxidase from the fungus curvularia inaequalis: recombinant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VNI
- Type
- protein
- Length
- 574 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vanadium chloroperoxidase
- EC
- 1.11.1.10
- UniProt
- P49053
- Ligands
- VO4
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vanadium chloroperoxidase (EC 1.11.1.10) | protein | 574 | 43% helix, 9% strand | P49053 |
Ligands and binding sites
- VO4 · Vanadate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1116 | 0.80 | 0.81 | 103 | VO4 |
| 2 | 104 | 0.52 | 0.82 | 21 | empty |
| 3 | 125 | 0.42 | 0.76 | 21 | empty |
| 4 | 57 | 0.32 | 0.77 | 18 | empty |
| 5 | 64 | 0.27 | 0.72 | 20 | empty |
Compared structures
- 1VNI · Chloroperoxidase from the fungus curvularia inaequalis: recombinant holo-chloroperoxidase · the same entry in another collection · chain A against A, TM-score 1.00
- P49053 · AlphaFold monomer V2.0 prediction for vanadium chloroperoxidase (P49053) · 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 P49053
- Elsewhere: RCSB PDB 1VNI · PDBe 1VNI · UniProt P49053
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