MolNFT v1 · #187343 · protein
Lrr-F-box plant ubiquitin ligase
7SA1: “Lrr-F-box plant ubiquitin ligase”. X-ray diffraction. MolNFT v1 #187343 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7SA1
- Type
- protein
- Length
- 1,494 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q39255, Q5VMP0
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 122 | — | Q39255 |
| B, D | — | protein | 624 | — | Q5VMP0 |
| C | — | protein | 124 | — | Q39255 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B, C
- CIT · Citric acid · additive · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7SA1 · LRR-F-Box plant ubiquitin ligase · the same entry in another collection · chain A against A, TM-score 1.00
- Q5VMP0 · AlphaFold monomer V2.0 prediction for F-BOX/LRR-repeat MAX2 homolog (Q5VMP0) · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q39255 · AlphaFold monomer V2.0 prediction for SKP1-like protein 1A (Q39255) · a predicted model of the same protein · chain C against A, TM-score 0.93
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 Q39255
- Every structure of UniProt Q5VMP0
- Elsewhere: RCSB PDB 7SA1 · PDBe 7SA1 · UniProt Q39255 · UniProt Q5VMP0
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