Research workbench
Crystal structure of arfgap and ank repeat domain of ACAP1
Analyse Crystal structure of arfgap and ank repeat domain of ACAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JUE
- Type
- protein
- Length
- 504 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arfgap with coiled-coil, ank repeat and pH domain- containing protein 1
- UniProt
- Q15027
- Ligands
- ZN, SO4
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arfgap with coiled-coil, ank repeat and pH domain- containing protein 1 | protein | 250 | 46% helix, 4% strand | Q15027 |
| B | Arfgap with coiled-coil, ank repeat and pH domain- containing protein 1 | protein | 254 | 48% helix, 4% strand | Q15027 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.57 | 0.76 | 40 | empty |
| 2 | 98 | 0.53 | 0.83 | 17 | empty |
| 3 | 104 | 0.48 | 0.80 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 456 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3JUE · Crystal Structure of ArfGAP and ANK repeat domain of ACAP1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q15027 · AlphaFold monomer V2.0 prediction for arf-gap with coiled-coil, ank repeat and pH… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q15027
- Elsewhere: RCSB PDB 3JUE · PDBe 3JUE · UniProt Q15027
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