Research workbench
Crystal structure of human acyl-CoA dehydrogenase 11
Analyse Crystal structure of human acyl-CoA dehydrogenase 11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WBI
- Type
- protein
- Length
- 792 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-CoA dehydrogenase family member 11
- UniProt
- Q709F0
- Ligands
- FAD, UNX, PO4
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-CoA dehydrogenase family member 11 | protein | 394 | 58% helix, 16% strand | Q709F0 |
| B | Acyl-CoA dehydrogenase family member 11 | protein | 398 | 58% helix, 16% strand | Q709F0 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- UNX · Unknown atom or ion · ion · 14 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1158 | 0.86 | 0.87 | 112 | FAD, UNX |
| 2 | 1091 | 0.86 | 0.87 | 99 | FAD, UNX |
| 3 | 77 | 0.53 | 0.86 | 28 | empty |
| 4 | 263 | 0.53 | 0.75 | 25 | empty |
| 5 | 104 | 0.47 | 0.80 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1896 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 2WBI · Crystal structure of human acyl-CoA dehydrogenase 11 · the same entry in another collection · chain A against A, TM-score 1.00
- Q709F0 · AlphaFold monomer V2.0 prediction for acyl-CoA dehydrogenase family member 11 (Q709F0) · 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 Q709F0
- Elsewhere: RCSB PDB 2WBI · PDBe 2WBI · UniProt Q709F0
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