Research workbench
Processive endocellulase celf of clostridium cellulolyticum
Analyse Processive endocellulase celf of clostridium cellulolyticum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FCE
- Type
- protein
- Length
- 629 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulase celf
- EC
- 3.2.1.4
- UniProt
- P37698
- Ligands
- MGL, SGC, BGC, CA
- Pockets
- 4 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulase celf (EC 3.2.1.4) | protein | 629 | 39% helix, 17% strand | P37698 |
Ligands and binding sites
- MGL · methyl beta-D-glucopyranoside · ligand · 2 copies · chains A
- SGC · 4-thio-beta-D-glucopyranose · ligand · 2 copies · chains A
- BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1076 | 0.87 | 0.88 | 100 | MGL, SGC, BGC |
| 2 | 74 | 0.49 | 0.83 | 25 | empty |
| 3 | 58 | 0.34 | 0.77 | 15 | empty |
| 4 | 57 | 0.31 | 0.76 | 13 | empty |
Compared structures
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 P37698
- Elsewhere: RCSB PDB 1FCE · PDBe 1FCE · UniProt P37698
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