Research workbench
A common protein fold and similar active site in two distinct families of beta-glycanases
Analyse A common protein fold and similar active site in two distinct families of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CEC
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase celc
- EC
- 3.2.1.4
- UniProt
- P07985
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase celc (EC 3.2.1.4) | protein | 331 | 45% helix, 15% strand | P07985 |
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 | 0.55 | 0.76 | 27 | empty |
| 2 | 85 | 0.38 | 0.76 | 18 | empty |
Compared structures
- 1CEC · A common protein fold and similar active site in two distinct families of beta-glycanases · 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 1CEC · PDBe 1CEC · UniProt P07985
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