Research workbench
Crystal structure of aspergillus fumigatus mitochondrial acetyl-CoA acetyltransferase
Analyse Crystal structure of aspergillus fumigatus mitochondrial acetyl-CoA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L2G
- Type
- protein
- Length
- 1,588 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA-acetyltransferase, putative
- UniProt
- B0XMC1
- Pockets
- 12 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Acetyl-CoA-acetyltransferase, putative | protein | 397 | 36% helix, 24% strand | B0XMC1 |
Pockets
12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.61 | 0.79 | 40 | empty |
| 2 | 250 | 0.61 | 0.80 | 40 | empty |
| 3 | 215 | 0.59 | 0.80 | 31 | empty |
| 4 | 257 | 0.59 | 0.79 | 38 | empty |
| 5 | 222 | 0.59 | 0.80 | 33 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2920 Ų buried · 63 hydrogen bonds · protein-protein
- A–B · 2914 Ų buried · 66 hydrogen bonds · protein-protein
- A–D · 683 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 658 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 298 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (acetylation).
Compared structures
- 6L2G · Crystal structure of Aspergillus fumigatus mitochondrial acetyl-CoA acetyltransferase · 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 B0XMC1
- Elsewhere: RCSB PDB 6L2G · PDBe 6L2G · UniProt B0XMC1
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