MolNFT v1 · #126165 · protein
Structure of a triple variant of cutinase 2 from thermobifida cellulosilytica
5LUL: “Structure of a triple variant of cutinase 2 from thermobifida cellulosilytica”. X-ray diffraction, 2 ligands (CA, CL), 1 pocket (best druggability 0.58). MolNFT v1 #126165 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5LUL
- Type
- protein
- Length
- 525 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cutinase 2
- UniProt
- E9LVH9
- Ligands
- CA, CL
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cutinase 2 | protein | 262 | 31% helix, 21% strand | E9LVH9 |
| B | Cutinase 2 | protein | 263 | 31% helix, 21% strand | E9LVH9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.58 | 0.83 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 549 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5LUL · Structure of a triple 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 5LUL · PDBe 5LUL · UniProt E9LVH9
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