Research workbench
Medium chain acyl-CoA dehydrogenase, K304E mutant
Analyse Medium chain acyl-CoA dehydrogenase, K304E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P13
- Type
- protein
- Length
- 1,546 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- EC
- 1.3.8.7
- UniProt
- P11310
- Ligands
- FAD
- Pockets
- 13 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.7) | protein | 387 | 57% helix, 17% strand | P11310 |
| B, D | Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.8.7) | protein | 386 | 57% helix, 17% strand | P11310 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 602 | 0.82 | 0.86 | 77 | FAD |
| 2 | 564 | 0.81 | 0.87 | 71 | FAD |
| 3 | 628 | 0.81 | 0.85 | 81 | FAD |
| 4 | 654 | 0.80 | 0.85 | 81 | FAD |
| 5 | 1172 | 0.79 | 0.81 | 95 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2478 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 2451 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1797 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 1786 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 194 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 P11310
- Elsewhere: RCSB PDB 4P13 · PDBe 4P13 · UniProt P11310
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