Research workbench
Benzoylsuccinyl-CoA thiolase
Analyse Benzoylsuccinyl-CoA thiolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PXP
- Type
- protein
- Length
- 2,074 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q39VG2, Q39VG1
- Ligands
- ZN
Structure
x-ray diffraction · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 132 | — | Q39VG2 |
| B, F | — | protein | 131 | — | Q39VG2 |
| C | — | protein | 384 | — | Q39VG1 |
| D | — | protein | 385 | — | Q39VG1 |
| E | — | protein | 133 | — | Q39VG2 |
| G | — | protein | 391 | — | Q39VG1 |
| H | — | protein | 387 | — | Q39VG1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PXP · Benzoylsuccinyl-CoA thiolase · the same entry in another collection · chain G against G, 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 Q39VG2
- Every structure of UniProt Q39VG1
- Elsewhere: RCSB PDB 7PXP · PDBe 7PXP · UniProt Q39VG2 · UniProt Q39VG1
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