Research workbench
Structure of the pn loop Q182A mutant C3BOT1 exoenzyme (free state, crystal form I)
Analyse Structure of the pn loop Q182A mutant C3BOT1 exoenzyme (free state, crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C8G
- Type
- protein
- Length
- 821 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
- SO4
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mono-ADP-ribosyltransferase C3 (EC 2.4.2.-) | protein | 207 | 36% helix, 26% strand | P15879 |
| B | Mono-ADP-ribosyltransferase C3 (EC 2.4.2.-) | protein | 202 | 36% helix, 26% strand | P15879 |
| C | Mono-ADP-ribosyltransferase C3 (EC 2.4.2.-) | protein | 208 | 35% helix, 25% strand | P15879 |
| D | Mono-ADP-ribosyltransferase C3 (EC 2.4.2.-) | protein | 204 | 36% helix, 25% strand | P15879 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains 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 | 636 | 0.78 | 0.83 | 51 | empty |
| 2 | 656 | 0.74 | 0.80 | 62 | empty |
| 3 | 438 | 0.65 | 0.78 | 53 | SO4 |
| 4 | 192 | 0.53 | 0.78 | 30 | SO4 |
| 5 | 156 | 0.50 | 0.78 | 23 | empty |
Interfaces
6 interfaces between chains.
- A–D · 518 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 409 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 408 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 257 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 245 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2C8G · Structure of the PN loop Q182A mutant C3bot1 Exoenzyme (Free state, crystal form I) · 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 2C8G · PDBe 2C8G · UniProt P15879
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