Research workbench
Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from prunus communis
Analyse Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CGS
- Type
- protein
- Length
- 516 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A5E4GBK6
- Ligands
- FAD, BCN, NAG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 516 | — | A0A5E4GBK6 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- BCN · Bicine · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CGS · Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from Prunus… · 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 A0A5E4GBK6
- Elsewhere: RCSB PDB 7CGS · PDBe 7CGS · UniProt A0A5E4GBK6
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