Research workbench
Benzylsuccinate alpha-gamma complex
Analyse Benzylsuccinate alpha-gamma complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PKC
- Type
- protein
- Length
- 884 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tutd; Tutf
- EC
- 4.1.99.11
- UniProt
- O68395, O68394
- Ligands
- CL
- Pockets
- 13 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tutd (EC 4.1.99.11) | protein | 843 | 50% helix, 8% strand | O68395 |
| C | Tutf (EC 4.1.99.11) | protein | 41 | 0% helix, 54% strand | O68394 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.73 | 0.85 | 45 | empty |
| 2 | 61 | 0.72 | 0.98 | 24 | CL |
| 3 | 114 | 0.65 | 0.89 | 24 | empty |
| 4 | 60 | 0.64 | 0.93 | 19 | empty |
| 5 | 152 | 0.58 | 0.82 | 31 | empty |
Interfaces
1 interface between chains.
- A–C · 1156 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 4PKC · Benzylsuccinate alpha-gamma complex · 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 O68395
- Every structure of UniProt O68394
- Elsewhere: RCSB PDB 4PKC · PDBe 4PKC · UniProt O68395 · UniProt O68394
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