MolNFT v1 · #115161 · protein
Calcium activated non-selective cation channel
5CBG · Ion transport 2 domain protein: “Calcium activated non-selective cation channel”. X-ray diffraction, 1 ligand (CA), 8 pockets (best druggability 0.74). MolNFT v1 #115161 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5CBG
- Type
- protein
- Length
- 612 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ion transport 2 domain protein
- UniProt
- D5UM26
- Ligands
- CA
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Ion transport 2 domain protein | protein | 102 | 65% helix, 0% strand | D5UM26 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, E, B, D, F
- DMU · Decyl-beta-D-maltopyranoside · additive · 3 copies · chains D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 510 | 0.74 | 0.83 | 71 | CA |
| 2 | 226 | 0.55 | 0.77 | 20 | empty |
| 3 | 191 | 0.53 | 0.77 | 19 | empty |
| 4 | 208 | 0.53 | 0.77 | 24 | empty |
| 5 | 205 | 0.52 | 0.76 | 20 | empty |
Interfaces
8 interfaces between chains.
- A–E · 1240 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 1213 Ų buried · 2 hydrogen bonds · protein-protein
- D–E · 1159 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 1117 Ų buried · 4 hydrogen bonds · protein-protein
- A–F · 182 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5CBG · Calcium activated non-selective cation channel · the same entry in another collection · chain D against D, TM-score 1.00
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 D5UM26
- Elsewhere: RCSB PDB 5CBG · PDBe 5CBG · UniProt D5UM26
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