MolNFT v1 · #136768 · protein
Novel structural insights into GDP-mediated regulation of acyl-CoA thioesterases
5V3A: “Novel structural insights into GDP-mediated regulation of acyl-CoA thioesterases”. X-ray diffraction, 2 ligands (COA, GDP). MolNFT v1 #136768 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5V3A
- Type
- protein
- Length
- 616 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0Y5D4F5
- Ligands
- COA, GDP
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 154 | — | A0A0Y5D4F5 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, B, C, D
- GDP · Guanosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5V3A · Novel Structural Insights into GDP-Mediated Regulation of Acyl-CoA Thioesterases · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0Y5D4F5
- Elsewhere: RCSB PDB 5V3A · PDBe 5V3A · UniProt A0A0Y5D4F5
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