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Crystal structure of murine ARL3-GDP
Analyse Crystal structure of murine ARL3-GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FZQ
- 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 3
- UniProt
- Q9WUL7
- Ligands
- GDP, SO4, NH4
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor-like protein 3 | protein | 176 | 34% helix, 26% strand | Q9WUL7 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- NH4 · Ammonium ion · ion · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q9WUL7
- Elsewhere: RCSB PDB 1FZQ · PDBe 1FZQ · UniProt Q9WUL7
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