MolNFT v1 · #63842 · protein
The crystal structure of human acyl-coenzymea binding domain containing 5
3FLV · Acyl-CoA-binding domain-containing protein 5: “The crystal structure of human acyl-coenzymea binding domain containing 5”. X-ray diffraction, 3 ligands (COA, STE, UNX), 2 pockets (best druggability 0.47). MolNFT v1 #63842 on…
- PDB
- 3FLV
- Type
- protein
- Length
- 181 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-CoA-binding domain-containing protein 5
- UniProt
- Q5T8D3
- Ligands
- COA, STE, UNX
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-CoA-binding domain-containing protein 5 | protein | 92 | 70% helix, 0% strand | Q5T8D3 |
| B | Acyl-CoA-binding domain-containing protein 5 | protein | 89 | 66% helix, 0% strand | Q5T8D3 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
- STE · Stearic acid · ligand
- UNX · Unknown atom or ion · ion · 4 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.47 | 0.74 | 27 | UNX |
| 2 | 84 | 0.33 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 192 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3FLV · The crystal structure of human acyl-CoenzymeA binding domain containing 5 · the same entry in another collection · chain A against A, TM-score 1.00
- Q5T8D3 · AlphaFold monomer V2.0 prediction for acyl-CoA-binding domain- containing protein 5… · 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 Q5T8D3
- Elsewhere: RCSB PDB 3FLV · PDBe 3FLV · UniProt Q5T8D3
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