Research workbench
Cellulase (celc) mutant with glu 140 replaced by gln complexed with cellohexaose
Analyse Cellulase (celc) mutant with glu 140 replaced by gln complexed with cellohexaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CEN
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulase celc
- EC
- 3.2.1.4
- UniProt
- P07985
- Ligands
- BGC
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulase celc (EC 3.2.1.4) | protein | 334 | 43% helix, 16% strand | P07985 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.53 | 0.75 | 34 | BGC |
| 2 | 117 | 0.46 | 0.78 | 20 | empty |
Compared structures
- 1CEN · Cellulase (celc) mutant with glu 140 replaced by gln complexed with cellohexaose · 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 P07985
- Elsewhere: RCSB PDB 1CEN · PDBe 1CEN · UniProt P07985
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.