Research workbench
Structure of SUR2B in complex with mg-ATP/ADP
Analyse Structure of SUR2B in complex with mg-ATP/ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VLR
- Type
- protein
- Length
- 1,145 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform SUR2B of ATP-binding cassette sub-family C member 9
- UniProt
- Q63563
- Ligands
- Y01, ADP, ATP, MG
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 65% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform SUR2B of ATP-binding cassette sub-family C member 9 | protein | 1145 | 65% helix, 11% strand | Q63563 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.84 | 0.96 | 36 | empty |
| 2 | 298 | 0.82 | 0.93 | 51 | empty |
| 3 | 205 | 0.79 | 0.93 | 48 | empty |
| 4 | 133 | 0.78 | 0.96 | 29 | empty |
| 5 | 149 | 0.74 | 0.92 | 27 | empty |
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 Q63563
- Elsewhere: RCSB PDB 7VLR · PDBe 7VLR · UniProt Q63563
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