Research workbench
Complex structure of mutant CTCEL5E (E314A) with cellobiose
Analyse Complex structure of mutant CTCEL5E (E314A) with cellobiose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U5K
- Type
- protein
- Length
- 602 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase H
- EC
- 3.2.1.4
- UniProt
- P16218
- Ligands
- BGC
- Pockets
- 5 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase H (EC 3.2.1.4) | protein | 304 | 39% helix, 18% strand | P16218 |
| B | Endoglucanase H (EC 3.2.1.4) | protein | 298 | 41% helix, 18% strand | P16218 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.60 | 0.84 | 25 | empty |
| 2 | 233 | 0.51 | 0.75 | 33 | BGC |
| 3 | 86 | 0.41 | 0.79 | 19 | empty |
| 4 | 94 | 0.37 | 0.75 | 15 | BGC |
| 5 | 74 | 0.33 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1560 Ų buried · 18 hydrogen bonds · protein-protein
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 P16218
- Elsewhere: RCSB PDB 4U5K · PDBe 4U5K · UniProt P16218
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