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Crystal structure of beta-ketoadipyl-CoA thiolase mutant (H356A) in complex with CoA
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
- 6PCB
- Type
- protein
- Length
- 1,599 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q88N39
- Ligands
- COA, CL
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 403 | — | Q88N39 |
| B, C | — | protein | 397 | — | Q88N39 |
| D | — | protein | 402 | — | Q88N39 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 5 copies · chains A, B, C, D
- 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
- 6PCB · Crystal structure of beta-ketoadipyl-CoA thiolase mutant (H356A) in complex with COA · 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 6PCB · PDBe 6PCB · UniProt Q88N39
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