Research workbench
Partition protein-ADP complex
Analyse Partition protein-ADP complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EZ2
- Type
- protein
- Length
- 782 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plasmid partition protein a
- UniProt
- P07620
- Ligands
- ADP, MG
- Pockets
- 6 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Plasmid partition protein a | protein | 388 | 52% helix, 12% strand | P07620 |
| B | Plasmid partition protein a | protein | 394 | 53% helix, 13% strand | P07620 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.80 | 0.82 | 91 | ADP, MG |
| 2 | 249 | 0.71 | 0.86 | 41 | ADP |
| 3 | 319 | 0.64 | 0.80 | 29 | empty |
| 4 | 94 | 0.42 | 0.78 | 24 | empty |
| 5 | 60 | 0.33 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2795 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
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 P07620
- Elsewhere: RCSB PDB 3EZ2 · PDBe 3EZ2 · UniProt P07620
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