MolNFT v1 · #8390 · protein
Structure of the clostridium botulinum C3 exoenzyme (L177C mutant)
1GZE · Mono-ADP-ribosyltransferase C3: “Structure of the clostridium botulinum C3 exoenzyme (L177C mutant)”. X-ray diffraction, 1 ligand (HG), 10 pockets (best druggability 0.73). MolNFT v1 #8390 on GenesisL1: 3D structure, binding sites…
- PDB
- 1GZE
- Type
- protein
- Length
- 823 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mono-ADP-ribosyltransferase C3
- EC
- 2.4.2.-
- UniProt
- P15879
- Ligands
- HG
- Pockets
- 10 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mono-ADP-ribosyltransferase C3 (EC 2.4.2.-) | protein | 207 | 29% helix, 24% strand | P15879 |
| B, D | Mono-ADP-ribosyltransferase C3 (EC 2.4.2.-) | protein | 203 | 33% helix, 28% strand | P15879 |
| C | Mono-ADP-ribosyltransferase C3 (EC 2.4.2.-) | protein | 210 | 32% helix, 23% strand | P15879 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 675 | 0.73 | 0.80 | 43 | empty |
| 2 | 468 | 0.69 | 0.80 | 63 | empty |
| 3 | 182 | 0.56 | 0.80 | 26 | empty |
| 4 | 222 | 0.53 | 0.77 | 36 | empty |
| 5 | 134 | 0.51 | 0.80 | 32 | empty |
Interfaces
6 interfaces between chains.
- A–D · 545 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 371 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 360 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 295 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 248 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1GZE · Structure of the Clostridium botulinum C3 exoenzyme (L177C mutant) · 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 P15879
- Elsewhere: RCSB PDB 1GZE · PDBe 1GZE · UniProt P15879
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