MolNFT v1 · #150587 · protein
Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide
6GY5: “Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide”. X-ray diffraction, 2 ligands (NA, CL). MolNFT v1 #150587 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GY5
- Type
- protein
- Length
- 296 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y2M5
- Ligands
- NA, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 285 | — | Q9Y2M5 |
| U | — | protein | 11 | — | — |
Ligands and binding sites
- NA · Sodium ion · metal · 14 copies · chains A, U
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, U
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GY5 · Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y2M5 · AlphaFold monomer V2.0 prediction for kelch-like protein 20 (Q9Y2M5) · 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 Q9Y2M5
- Elsewhere: RCSB PDB 6GY5 · PDBe 6GY5 · UniProt Q9Y2M5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.