Research workbench
1.46 a resolution structure of PHND1 from prochlorococcus marinus (mit 9301) in complex with phosphite
Analyse 1.46 a resolution structure of PHND1 from prochlorococcus marinus (mit 9301) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LQ5
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A3PC74
- Ligands
- PO3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 274 | — | A3PC74 |
Ligands and binding sites
- PO3 · Phosphite ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LQ5 · 1.46 A resolution structure of PhnD1 from Prochlorococcus marinus (MIT 9301) in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- A3PC74 · AlphaFold monomer V2.0 prediction for probable ABC transporter phosphite binding protein… · a predicted model of the same protein · chain A 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 A3PC74
- Elsewhere: RCSB PDB 5LQ5 · PDBe 5LQ5 · UniProt A3PC74
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