Research workbench
Multifunctional cellulase, xylanase, mannanase
Analyse Multifunctional cellulase, xylanase, mannanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IM4
- Type
- protein
- Length
- 2,016 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase E
- EC
- 3.2.1.4
- UniProt
- P10477
- Pockets
- 13 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Endoglucanase E (EC 3.2.1.4) | protein | 336 | 40% helix, 13% strand | P10477 |
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.74 | 0.80 | 74 | empty |
| 2 | 475 | 0.72 | 0.81 | 70 | empty |
| 3 | 425 | 0.60 | 0.75 | 44 | empty |
| 4 | 264 | 0.53 | 0.76 | 31 | empty |
| 5 | 281 | 0.53 | 0.75 | 32 | empty |
Interfaces
7 interfaces between chains.
- A–E · 564 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 550 Ų buried · 6 hydrogen bonds · protein-protein
- A–F · 518 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 478 Ų buried · 6 hydrogen bonds · protein-protein
- B–E · 449 Ų buried · 6 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 P10477
- Elsewhere: RCSB PDB 4IM4 · PDBe 4IM4 · UniProt P10477
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