MolNFT v1 · #61534 · protein
Complex of ARL2 and bart, crystal form 2
3DOF · ADP-ribosylation factor-like protein 2: “Complex of ARL2 and bart, crystal form 2”. X-ray diffraction, 2 ligands (GTP, MG), 2 pockets (best druggability 0.70). MolNFT v1 #61534 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3DOF
- Type
- protein
- Length
- 309 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor-like protein 2; ADP-ribosylation factor-like protein 2-binding…
- UniProt
- P36404, Q9Y2Y0
- Ligands
- GTP, MG
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor-like protein 2 | protein | 189 | 35% helix, 23% strand | P36404 |
| B | ADP-ribosylation factor-like protein 2-binding protein | protein | 120 | 60% helix, 1% strand | Q9Y2Y0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.70 | 0.83 | 33 | empty |
| 2 | 104 | 0.43 | 0.78 | 25 | GTP, MG |
Interfaces
1 interface between chains.
- A–B · 1142 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3DOF · Complex of ARL2 and BART, Crystal Form 2 · the same entry in another collection · chain A against A, TM-score 1.00
- P36404 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-like protein 2 (P36404) · a predicted model of the same protein · chain A against A, TM-score 0.90
- Q9Y2Y0 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-like protein 2-binding… · a predicted model of the same protein · chain B against A, TM-score 0.85
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 P36404
- Every structure of UniProt Q9Y2Y0
- Elsewhere: RCSB PDB 3DOF · PDBe 3DOF · UniProt P36404 · UniProt Q9Y2Y0
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