Research workbench
Cryo-EM structure of human CALHM2 in a ruthenium red-bound inhibited state
Analyse Cryo-EM structure of human CALHM2 in a ruthenium red-bound inhibited state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UIW
- Type
- protein
- Length
- 3,234 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9HA72
- Ligands
- R2R
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K | — | protein | 294 | — | Q9HA72 |
Ligands and binding sites
- R2R · ruthenium(6+) azanide pentaamino(oxido)ruthenium (1/4/2) · ligand · 11 copies · chains A, B, C, D, E, F, G, H, I, J, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UIW · Cryo-EM structure of human CALHM2 in a ruthenium red-bound inhibited state · the same entry in another collection · chain K against K, TM-score 1.00
- Q9HA72 · AlphaFold monomer V2.0 prediction for calcium homeostasis modulator protein 2 (Q9HA72) · a predicted model of the same protein · chain K against A, TM-score 0.84
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 Q9HA72
- Elsewhere: RCSB PDB 6UIW · PDBe 6UIW · UniProt Q9HA72
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