MolNFT v1 · #178844 · protein
The structure of CBM32-1 and CBM32-2 domains from clostridium perfringens zmpb in complex with galnac
7JNF · F5/8 type C domain protein: “The structure of CBM32-1 and CBM32-2 domains from clostridium perfringens zmpb in complex with galnac”. X-ray diffraction, 2 ligands (A2G, CA), 1 pocket (best druggability 0.38). MolNFT v1 #178844 on…
- PDB
- 7JNF
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F5/8 type C domain protein
- UniProt
- A0A0H2YN38
- Ligands
- A2G, CA
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F5/8 type C domain protein | protein | 398 | 19% helix, 39% strand | A0A0H2YN38 |
Ligands and binding sites
- A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- GOL · Glycerol · additive · 4 copies · chains A
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 | 90 | 0.38 | 0.76 | 23 | empty |
Compared structures
- 7JNF · The structure of CBM32-1 and CBM32-2 domains from Clostridium perfringens ZmpB in complex… · 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 A0A0H2YN38
- Elsewhere: RCSB PDB 7JNF · PDBe 7JNF · UniProt A0A0H2YN38
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.