Research workbench
The crac channel orai in an unlatched-closed conformation; K163W loss- of-function mutation
Analyse The crac channel orai in an unlatched-closed conformation; K163W loss… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BBH
- Type
- protein
- Length
- 3,600 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium release-activated calcium channel protein 1
- UniProt
- Q9U6B8
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 92% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X | Calcium release-activated calcium channel protein 1 | protein | 150 | 92% helix, 0% strand | Q9U6B8 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.87 | 0.97 | 36 | empty |
| 2 | 293 | 0.86 | 0.96 | 36 | empty |
| 3 | 535 | 0.85 | 0.90 | 57 | empty |
| 4 | 541 | 0.83 | 0.88 | 57 | empty |
| 5 | 550 | 0.72 | 0.80 | 67 | empty |
Interfaces
63 interfaces between chains.
- P–Q · 1910 Ų buried · 5 hydrogen bonds · protein-protein
- S–X · 1891 Ų buried · 4 hydrogen bonds · protein-protein
- S–T · 1881 Ų buried · 5 hydrogen bonds · protein-protein
- N–O · 1872 Ų buried · 4 hydrogen bonds · protein-protein
- G–L · 1870 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6BBH · The CRAC channel Orai in an unlatched-closed conformation; K163W loss-of-function mutation · the same entry in another collection · chain I against I, 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 Q9U6B8
- Elsewhere: RCSB PDB 6BBH · PDBe 6BBH · UniProt Q9U6B8
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