Research workbench
Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin cdta from clostridium difficile
Analyse Structural basis for substrate recognition in the enzymatic component of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WN5
- Type
- protein
- Length
- 394 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosyltransferase enzymatic component
- UniProt
- Q9KH42
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosyltransferase enzymatic component | protein | 394 | 38% helix, 28% strand | Q9KH42 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.55 | 0.77 | 39 | empty |
| 2 | 329 | 0.54 | 0.74 | 42 | empty |
| 3 | 103 | 0.53 | 0.83 | 24 | empty |
| 4 | 248 | 0.51 | 0.75 | 27 | empty |
| 5 | 68 | 0.29 | 0.74 | 9 | empty |
Compared structures
- 2WN5 · Structural Basis for Substrate Recognition in the Enzymatic Component of… · 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 Q9KH42
- Elsewhere: RCSB PDB 2WN5 · PDBe 2WN5 · UniProt Q9KH42
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