Research workbench
Structure of flen-amppnp complex
Analyse Structure of flen-amppnp complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J1J
- Type
- protein
- Length
- 521 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Site-determining protein
- UniProt
- G3XD64
- Ligands
- ANP, MG, SO4
- Pockets
- 5 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Site-determining protein | protein | 273 | 42% helix, 20% strand | G3XD64 |
| B | Site-determining protein | protein | 248 | 49% helix, 20% strand | G3XD64 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 845 | 0.88 | 0.90 | 104 | ANP, MG, SO4 |
| 2 | 195 | 0.60 | 0.81 | 23 | empty |
| 3 | 103 | 0.48 | 0.80 | 18 | empty |
| 4 | 172 | 0.42 | 0.73 | 27 | empty |
| 5 | 144 | 0.37 | 0.72 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1563 Ų buried · 15 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 G3XD64
- Elsewhere: RCSB PDB 5J1J · PDBe 5J1J · UniProt G3XD64
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