Research workbench
Structure of human ADP-ribosylation factor-like 8A binding to GDP
Analyse Structure of human ADP-ribosylation factor-like 8A binding to GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ILE
- Type
- protein
- Length
- 176 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor-like protein 8A
- UniProt
- Q96BM9
- Ligands
- GDP
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor-like protein 8A | protein | 176 | 36% helix, 23% strand | Q96BM9 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4ILE · Structure of human ADP-ribosylation factor-like 8A binding to GDP · the same entry in another collection · chain A against A, TM-score 1.00
- Q96BM9 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-like protein 8A (Q96BM9) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 Q96BM9
- Elsewhere: RCSB PDB 4ILE · PDBe 4ILE · UniProt Q96BM9
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