Research workbench
Crystal structure of pH domain of OSH3 from saccharomyces cerevisiae
Analyse Crystal structure of pH domain of OSH3 from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IAP
- Type
- protein
- Length
- 512 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxysterol-binding protein homolog 3,ENDOLYSIN,OXYSTEROL- binding protein homolog 3
- EC
- 3.2.1.17
- UniProt
- P38713, P00720
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Oxysterol-binding protein homolog 3,ENDOLYSIN,OXYSTEROL- binding protein homolog 3 (EC 3.2.1.17) | protein | 256 | 46% helix, 21% strand | P38713, P00720 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 787 | 0.69 | 0.76 | 75 | SO4 |
| 2 | 197 | 0.48 | 0.75 | 31 | empty |
| 3 | 116 | 0.41 | 0.76 | 17 | SO4 |
| 4 | 57 | 0.40 | 0.81 | 18 | empty |
| 5 | 65 | 0.38 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1235 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4IAP · Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- P38713 · AlphaFold monomer V2.0 prediction for oxysterol-binding protein homolog 3 (P38713) · a predicted model of the same protein · chain A against A, TM-score 0.32
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 P38713
- Every structure of UniProt P00720
- Elsewhere: RCSB PDB 4IAP · PDBe 4IAP · UniProt P38713 · UniProt P00720
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