Research workbench
HBEST2 CA2+-unbound closed state
Analyse HBEST2 CA2+-unbound closed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8D1H
- Type
- protein
- Length
- 1,880 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8NFU1
- Ligands
- MC3, DU0, CL
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, B, A, C, D | — | protein | 376 | — | Q8NFU1 |
Ligands and binding sites
- MC3 · 1,2-dimyristoyl-rac-glycero-3-phosphocholine · ligand · 45 copies · chains E, A, B, C, D
- DU0 · 2-[2-[(1~{S},2~{S},4~{S},5'~{R},6~{R},7~{S},8~{R}, 9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4, 8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxyethyl]propane-1,3-diol · ligand · 5 copies · chains E, B, A, C, D
- CL · Chloride ion · ion · chains E, B, A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q8NFU1
- Elsewhere: RCSB PDB 8D1H · PDBe 8D1H · UniProt Q8NFU1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.