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
- 2ZUM
- Type
- protein
- Length
- 377 residues
- Chains
- 1
- 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
- ZN
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 30% 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 | 30% helix, 16% strand | O58925 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A
- GOL · Glycerol · additive · 8 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 223 | 0.50 | 0.75 | 27 | ACT, ZN, GOL |
| 2 | 52 | 0.26 | 0.74 | 11 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2ZUM · 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 2ZUM · PDBe 2ZUM · UniProt O58925
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