MolNFT v1 · #16816 · protein
Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability
1OA4 · Endo-beta-1,4-glucanase: “Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability”. X-ray diffraction, 1 pocket (best druggability 0.57). MolNFT v1 #16816 on GenesisL1: 3D structure…
- PDB
- 1OA4
- Type
- protein
- Length
- 222 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-beta-1,4-glucanase
- EC
- 3.2.1.4
- UniProt
- Q9KIH1
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-beta-1,4-glucanase (EC 3.2.1.4) | protein | 222 | 6% helix, 50% strand | Q9KIH1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.57 | 0.80 | 42 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1OA4 · Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for… · 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 Q9KIH1
- Elsewhere: RCSB PDB 1OA4 · PDBe 1OA4 · UniProt Q9KIH1
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