Research workbench
Crystal structure of a hypothetical protein at 2.0 a resolution
Analyse Crystal structure of a hypothetical protein at 2.0 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SUM
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphate transport system protein phou homolog 2
- UniProt
- Q9X256
- Ligands
- FE, NI, CA, PO3
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Phosphate transport system protein phou homolog 2 | protein | 225 | 82% helix, 4% strand | Q9X256 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 7 copies · chains B
- NI · Nickel (II) ion · metal · chains B
- CA · Calcium ion · metal · chains B
- PO3 · Phosphite ion · ion · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1SUM · Crystal structure of a hypothetical protein at 2.0 A resolution · the same entry in another collection · chain B against B, TM-score 1.00
- Q9X256 · AlphaFold monomer V2.0 prediction for phosphate-specific transport system accessory… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9X256
- Elsewhere: RCSB PDB 1SUM · PDBe 1SUM · UniProt Q9X256
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.