MolNFT v1 · #169668 · protein
Human atlastin-3 (residues 1-334) bound to GDP-MG2+ exhibits an ordered amino terminus
6XJO: “Human atlastin-3 (residues 1-334) bound to GDP-MG2+ exhibits an ordered amino terminus”. X-ray diffraction, 2 ligands (GDP, MG). MolNFT v1 #169668 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XJO
- Type
- protein
- Length
- 621 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6DD88
- Ligands
- GDP, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 326 | — | Q6DD88 |
| B | — | protein | 295 | — | Q6DD88 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XJO · Human atlastin-3 (residues 1-334) bound to GDP-Mg2+ exhibits an ordered amino terminus · the same entry in another collection · chain B against B, TM-score 1.00
- Q6DD88 · AlphaFold monomer V2.0 prediction for atlastin-3 (Q6DD88) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q6DD88
- Elsewhere: RCSB PDB 6XJO · PDBe 6XJO · UniProt Q6DD88
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