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Crystal structure of ARF6DELTA13 complexed with GDP
Analyse Crystal structure of ARF6DELTA13 complexed with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N5C
- Type
- protein
- Length
- 307 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor 6
- UniProt
- P62330
- Ligands
- GDP, CL
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor 6 | protein | 147 | 36% helix, 24% strand | P62330 |
| B | ADP-ribosylation factor 6 | protein | 160 | 32% helix, 23% strand | P62330 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.45 | 0.80 | 24 | empty |
| 2 | 75 | 0.36 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1525 Ų buried · 17 hydrogen bonds · protein-protein
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 P62330
- Elsewhere: RCSB PDB 3N5C · PDBe 3N5C · UniProt P62330
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