Research workbench
C-terminal peptide depleted mutant of hydroxynitrile lyase from passiflora edulis (pehnl) bound with (R)-mandelonitrile
Analyse C-terminal peptide depleted mutant of hydroxynitrile lyase from passiflora… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y02
- Type
- protein
- Length
- 1,251 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1L7NZN4
- Ligands
- MXN, HBX
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, G, J, L | — | protein | 104 | — | A0A1L7NZN4 |
| C | — | protein | 107 | — | A0A1L7NZN4 |
| D, H, I | — | protein | 105 | — | A0A1L7NZN4 |
| E, F, K | — | protein | 103 | — | A0A1L7NZN4 |
Ligands and binding sites
- MXN · (2R)-hydroxy(phenyl)ethanenitrile · ligand · 4 copies · chains A, B, C, D, E, F, K, L
- HBX · benzaldehyde · ligand · 2 copies · chains I, L
- HEZ · Hexane-1,6-diol · additive · 9 copies · chains A, B, C, D, E, F, G, H, I, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5Y02 · C-terminal peptide depleted mutant of hydroxynitrile lyase from Passiflora edulis (PeHNL)… · 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 A0A1L7NZN4
- Elsewhere: RCSB PDB 5Y02 · PDBe 5Y02 · UniProt A0A1L7NZN4
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