Research workbench
The complex structure of C3CER exoenzyme and GTP bound rhoa (NADH- bound state)
Analyse The complex structure of C3CER exoenzyme and GTP bound rhoa (NADH- bound state) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XSH
- Type
- protein
- Length
- 382 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein rhoa; ADP-ribosyltransferase
- UniProt
- P61586, Q8KNY0
- Ligands
- GSP, NAI, MG
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming protein rhoa | protein | 177 | 38% helix, 23% strand | P61586 |
| B | ADP-ribosyltransferase | protein | 205 | 31% helix, 28% strand | Q8KNY0 |
Ligands and binding sites
- GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · chains A
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains A, B
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 594 | 0.78 | 0.83 | 59 | NAI, EDO |
| 2 | 109 | 0.76 | 0.96 | 23 | empty |
| 3 | 354 | 0.66 | 0.80 | 49 | GSP, MG |
| 4 | 90 | 0.40 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1175 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4XSH · The complex structure of C3cer exoenzyme and GTP bound RhoA (NADH-bound state) · the same entry in another collection · chain B against B, TM-score 1.00
- P61586 · AlphaFold monomer V2.0 prediction for transforming protein rhoa (P61586) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P61586
- Every structure of UniProt Q8KNY0
- Elsewhere: RCSB PDB 4XSH · PDBe 4XSH · UniProt P61586 · UniProt Q8KNY0
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