MolNFT v1 · #74983 · protein
Structure of espg-ARF6 complex
3PCR: “Structure of espg-ARF6 complex”. X-ray diffraction, 2 ligands (GTP, MG), 8 pockets (best druggability 0.64). MolNFT v1 #74983 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3PCR
- Type
- protein
- Length
- 509 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Espg; ADP-ribosylation factor 6
- UniProt
- Q7DB50, P62330
- Ligands
- GTP, MG
- Pockets
- 8 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Espg | protein | 349 | 32% helix, 26% strand | Q7DB50 |
| B | ADP-ribosylation factor 6 | protein | 160 | 29% helix, 26% strand | P62330 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 420 | 0.64 | 0.78 | 41 | GTP, MG |
| 2 | 61 | 0.52 | 0.86 | 13 | empty |
| 3 | 223 | 0.51 | 0.77 | 37 | empty |
| 4 | 189 | 0.46 | 0.75 | 32 | empty |
| 5 | 100 | 0.38 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 625 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
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 Q7DB50
- Every structure of UniProt P62330
- Elsewhere: RCSB PDB 3PCR · PDBe 3PCR · UniProt Q7DB50 · UniProt P62330
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