MolNFT v2 · #141752 · protein
p62/SQSTM1 ZZ domain with Ile-peptide
5YPH: “p62/SQSTM1 ZZ domain with Ile-peptide”. X-ray diffraction at 1.629, 1 ligand (ZN). MolNFT v2 #141752 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5YPH
- Type
- protein
- Length
- 100 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.629
- Source
- Homo sapiens
- UniProt
- P11021, Q13501
- Ligands
- ZN
Structure
x-ray diffraction · resolution 1.629 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 51 | — | P11021, Q13501 |
| B | — | protein | 49 | — | P11021, Q13501 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YPH · P62/SQSTM1 zz domain with ile-peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q13501 · AlphaFold monomer V2.0 prediction for sequestosome-1 (Q13501) · a predicted model of the same protein · chain B against A, TM-score 0.85
- P11021 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (P11021) · a predicted model of the same protein · chain B against A, TM-score 0.37
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 P11021
- Every structure of UniProt Q13501
- Elsewhere: RCSB PDB 5YPH · PDBe 5YPH · UniProt P11021 · UniProt Q13501
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