MolNFT v1 · #29746 · protein
Structure of truncated yeast oxysterol binding protein OSH4
1ZI7 · KES1 protein: “Structure of truncated yeast oxysterol binding protein OSH4”. X-ray diffraction, 1 ligand (SO4), 20 pockets (best druggability 0.74). MolNFT v1 #29746 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ZI7
- Type
- protein
- Length
- 1,198 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KES1 protein
- UniProt
- P35844
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | KES1 protein | protein | 402 | 27% helix, 32% strand | P35844 |
| B, C | KES1 protein | protein | 398 | 28% helix, 32% strand | P35844 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.74 | 0.81 | 57 | SO4 |
| 2 | 546 | 0.70 | 0.79 | 52 | empty |
| 3 | 310 | 0.69 | 0.83 | 50 | empty |
| 4 | 399 | 0.63 | 0.78 | 44 | empty |
| 5 | 430 | 0.63 | 0.77 | 50 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1079 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 334 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1ZI7 · Structure of truncated yeast oxysterol binding protein Osh4 · the same entry in another collection · chain A against A, TM-score 1.00
- P35844 · AlphaFold monomer V2.0 prediction for oxysterol-binding protein homolog 4 (P35844) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P35844
- Elsewhere: RCSB PDB 1ZI7 · PDBe 1ZI7 · UniProt P35844
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