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Crystal structure of malonyl CoA-acyl carrier protein transacylase from thermus thermophilus HB8
Analyse Crystal structure of malonyl CoA-acyl carrier protein transacylase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CUY
- Type
- protein
- Length
- 610 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Malonyl CoA-[acyl carrier protein] transacylase
- EC
- 2.3.1.39
- UniProt
- Q5SL77
- Pockets
- 3 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Malonyl CoA-[acyl carrier protein] transacylase (EC 2.3.1.39) | protein | 305 | 51% helix, 16% strand | Q5SL77 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1001 | 0.87 | 0.88 | 116 | empty |
| 2 | 299 | 0.67 | 0.82 | 49 | empty |
| 3 | 88 | 0.34 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1744 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2CUY · Crystal structure of malonyl CoA-acyl carrier protein transacylase from Thermus… · 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 Q5SL77
- Elsewhere: RCSB PDB 2CUY · PDBe 2CUY · UniProt Q5SL77
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