Research workbench
Crystal structure of arabidopsis thaliana PDX1K166R
Analyse Crystal structure of arabidopsis thaliana PDX1K166R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NHF
- Type
- protein
- Length
- 1,072 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8L940
- Ligands
- PO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 269 | — | Q8L940 |
| B | — | protein | 270 | — | Q8L940 |
| C | — | protein | 266 | — | Q8L940 |
| D | — | protein | 267 | — | Q8L940 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NHF · Crystal structure of Arabidopsis thaliana Pdx1K166R · the same entry in another collection · chain D against D, TM-score 1.00
- Q8L940 · AlphaFold monomer V2.0 prediction for pyridoxal 5'-phosphate synthase subunit PDX1.3… · a predicted model of the same protein · chain D 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 Q8L940
- Elsewhere: RCSB PDB 7NHF · PDBe 7NHF · UniProt Q8L940
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