Research workbench
Structure of a double variant of cutinase 2 from thermobifida cellulosilytica
Analyse Structure of a double variant of cutinase 2 from thermobifida cellulosilytica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LUK
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase 2
- UniProt
- E9LVH9
- Ligands
- MG, CL
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cutinase 2 | protein | 263 | 33% helix, 22% strand | E9LVH9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5LUK · Structure of a double variant of cutinase 2 from Thermobifida cellulosilytica · 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 E9LVH9
- Elsewhere: RCSB PDB 5LUK · PDBe 5LUK · UniProt E9LVH9
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