Research workbench
Complex structure of OSYCHF1 with AMP-pnp
Analyse Complex structure of OSYCHF1 with AMP-pnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EE3
- Type
- protein
- Length
- 721 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Obg-like ATPase 1
- EC
- 3.6.5.-
- UniProt
- Q6Z1J6
- Ligands
- ANP, MG, CL, SO4
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Obg-like ATPase 1 (EC 3.6.5.-) | protein | 357 | 46% helix, 19% strand | Q6Z1J6 |
| B | Obg-like ATPase 1 (EC 3.6.5.-) | protein | 364 | 46% helix, 19% strand | Q6Z1J6 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 6 copies · chains A, B
- SO4 · Sulfate ion · ion
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.75 | 0.94 | 29 | empty |
| 2 | 69 | 0.62 | 0.91 | 17 | empty |
| 3 | 63 | 0.48 | 0.84 | 23 | empty |
| 4 | 154 | 0.43 | 0.74 | 22 | empty |
| 5 | 134 | 0.41 | 0.74 | 16 | empty |
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 Q6Z1J6
- Elsewhere: RCSB PDB 5EE3 · PDBe 5EE3 · UniProt Q6Z1J6
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