Research workbench
Functional analysis of hyperthermophilic endocellulase from the archaeon pyrococcus horikoshii
Analyse Functional analysis of hyperthermophilic endocellulase from the archaeon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AXX
- Type
- protein
- Length
- 1,134 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 458AA long hypothetical endo-1,4-beta-glucanase
- EC
- 3.2.1.4
- UniProt
- O58925
- Ligands
- BGC, PO4
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 458AA long hypothetical endo-1,4-beta-glucanase (EC 3.2.1.4) | protein | 377 | 31% helix, 16% strand | O58925 |
| B | 458AA long hypothetical endo-1,4-beta-glucanase (EC 3.2.1.4) | protein | 379 | 31% helix, 17% strand | O58925 |
| C | 458AA long hypothetical endo-1,4-beta-glucanase (EC 3.2.1.4) | protein | 378 | 31% helix, 16% strand | O58925 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 6 copies · chains A, B, C
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1060 | 0.81 | 0.82 | 107 | BGC, PO4 |
| 2 | 341 | 0.63 | 0.79 | 45 | empty |
| 3 | 277 | 0.62 | 0.80 | 39 | empty |
| 4 | 92 | 0.49 | 0.82 | 20 | empty |
| 5 | 174 | 0.48 | 0.76 | 26 | BGC |
Interfaces
3 interfaces between chains.
- B–C · 808 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 520 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 232 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3AXX · Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus… · 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 O58925
- Elsewhere: RCSB PDB 3AXX · PDBe 3AXX · UniProt O58925
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