Research workbench
Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase
Analyse Structural basis for substrate fatty-acyl chain specificity: crystal structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B96
- Type
- protein
- Length
- 554 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Very long-chain specific acyl-CoA dehydrogenase
- EC
- 1.3.99.-
- UniProt
- P49748
- Ligands
- MYA, FAD
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Very long-chain specific acyl-CoA dehydrogenase (EC 1.3.99.-) | protein | 554 | 62% helix, 12% strand | P49748 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 599 | 0.79 | 0.84 | 72 | MYA, FAD |
| 2 | 244 | 0.52 | 0.76 | 24 | empty |
| 3 | 197 | 0.51 | 0.77 | 29 | empty |
| 4 | 51 | 0.39 | 0.81 | 16 | empty |
| 5 | 65 | 0.34 | 0.77 | 22 | empty |
Compared structures
- 3B96 · Structural Basis for Substrate Fatty-Acyl Chain Specificity: Crystal Structure of Human… · the same entry in another collection · chain A against A, TM-score 1.00
- P49748 · AlphaFold monomer V2.0 prediction for very long-chain specific acyl- CoA dehydrogenase… · a predicted model of the same protein · 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 P49748
- Elsewhere: RCSB PDB 3B96 · PDBe 3B96 · UniProt P49748
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