MolNFT v1 · #56425 · protein
Family 16 cabohydrate binding domain module 1
2ZEW · S-layer associated multidomain endoglucanase: “Family 16 cabohydrate binding domain module 1”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.34). MolNFT v1 #56425 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2ZEW
- Type
- protein
- Length
- 293 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-layer associated multidomain endoglucanase
- UniProt
- Q9ZA17
- Ligands
- CA
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-layer associated multidomain endoglucanase | protein | 146 | 2% helix, 49% strand | Q9ZA17 |
| B | S-layer associated multidomain endoglucanase | protein | 147 | 2% helix, 49% strand | Q9ZA17 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.34 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 759 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2ZEW · Family 16 Cabohydrate Binding Domain Module 1 · 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 Q9ZA17
- Elsewhere: RCSB PDB 2ZEW · PDBe 2ZEW · UniProt Q9ZA17
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.