Research workbench
Cryo-EM structure of the crac channel orai in an open conformation; H206A gain-of-function mutation in complex with an antibody
Analyse Cryo-EM structure of the crac channel orai in an open conformation; H206A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KR5
- Type
- protein
- Length
- 1,438 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium release-activated calcium channel protein 1; 19B5 Fab heavy chain; 19B5 Fab light…
- UniProt
- Q9U6B8
- Ligands
- CA
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 5 distinct chains · 20% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Calcium release-activated calcium channel protein 1 | protein | 127 | 83% helix, 0% strand | Q9U6B8 |
| H | 19B5 Fab heavy chain | protein | 116 | 3% helix, 50% strand | — |
| L, N, P | 19B5 Fab light chain | protein | 109 | 0% helix, 39% strand | — |
| M | 19B5 Fab heavy chain | protein | 116 | 3% helix, 51% strand | — |
| O | 19B5 Fab heavy chain | protein | 117 | 3% helix, 49% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · chains A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 709 | 0.77 | 0.81 | 57 | CA |
| 2 | 361 | 0.64 | 0.79 | 47 | empty |
| 3 | 277 | 0.64 | 0.81 | 43 | empty |
| 4 | 326 | 0.63 | 0.79 | 43 | empty |
| 5 | 124 | 0.60 | 0.85 | 26 | empty |
Interfaces
24 interfaces between chains.
- E–F · 1422 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 1419 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 1393 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 1116 Ų buried · 3 hydrogen bonds · protein-protein
- A–F · 1100 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 7KR5 · Cryo-EM structure of the CRAC channel Orai in an open conformation; H206A… · the same entry in another collection · chain P against P, 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 7KR5 · PDBe 7KR5 · UniProt Q9U6B8
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