Research workbench
Cellulase (celc) mutant with glu 140 replaced by gln
Analyse Cellulase (celc) mutant with glu 140 replaced by gln in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CEO
- Type
- protein
- Length
- 332 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
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulase celc (EC 3.2.1.4) | protein | 332 | 45% helix, 17% strand | P07985 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 343 | 0.57 | 0.76 | 32 | empty |
| 2 | 71 | 0.39 | 0.78 | 19 | empty |
| 3 | 58 | 0.38 | 0.80 | 16 | empty |
Compared structures
- 1CEO · Cellulase (celc) mutant with glu 140 replaced by gln · 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 1CEO · PDBe 1CEO · UniProt P07985
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