Research workbench
Structure of human ORP3 ord domain in complex with PI(4)P
Analyse Structure of human ORP3 ord domain in complex with PI(4)P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DEI
- Type
- protein
- Length
- 753 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9H4L5
- Ligands
- PIF
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 376 | — | Q9H4L5 |
| B | — | protein | 377 | — | Q9H4L5 |
Ligands and binding sites
- PIF · (2R)-3-{[(S)-hydroxy{[(1r,2r,3r,4r,5s,6r)-2,3,5,6-tetrahydroxy-4-(phosphonooxy) cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dioctanoate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7DEI · Structure of human ORP3 ORD domain in complex with PI(4)P · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H4L5 · AlphaFold monomer V2.0 prediction for oxysterol-binding protein- related protein 3… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q9H4L5
- Elsewhere: RCSB PDB 7DEI · PDBe 7DEI · UniProt Q9H4L5
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