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Crystal structure of beta-ketoadipyl-CoA thiolase mutant (H356A) in complex hexanoyl coenzyme a
Analyse Crystal structure of beta-ketoadipyl-CoA thiolase mutant (H356A) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PCC
- Type
- protein
- Length
- 1,599 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q88N39
- Ligands
- COA, O8Y
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 403 | — | Q88N39 |
| B | — | protein | 398 | — | Q88N39 |
| C | — | protein | 396 | — | Q88N39 |
| D | — | protein | 402 | — | Q88N39 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, B, C, D
- O8Y · hexanal · ligand · 4 copies · chains A, D, B, C
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PCC · Crystal structure of beta-ketoadipyl-CoA thiolase mutant (H356A) in complex hexanoyl… · 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 Q88N39
- Elsewhere: RCSB PDB 6PCC · PDBe 6PCC · UniProt Q88N39
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