MolNFT v1 · #138370 · protein
Cellulase CEL5C_N
5WH8 · Putative carbohydrate-active enzyme: “Cellulase CEL5C_N”. X-ray diffraction, 1 pocket (best druggability 0.39). MolNFT v1 #138370 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5WH8
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative carbohydrate-active enzyme
- UniProt
- E9NSK2
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative carbohydrate-active enzyme | protein | 323 | 36% helix, 17% strand | E9NSK2 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 13 copies · chains A
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.39 | 0.77 | 21 | EDO |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5WH8 · Cellulase Cel5C_n · 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 E9NSK2
- Elsewhere: RCSB PDB 5WH8 · PDBe 5WH8 · UniProt E9NSK2
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