Research workbench
Human ABCC6 NBD2 in ADP-bound state
Analyse Human ABCC6 NBD2 in ADP-bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BZR
- Type
- protein
- Length
- 473 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug resistance-associated protein 6
- UniProt
- O95255
- Ligands
- ADP
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Multidrug resistance-associated protein 6 | protein | 237 | 36% helix, 24% strand | O95255 |
| A | Multidrug resistance-associated protein 6 | protein | 236 | 37% helix, 25% strand | O95255 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains B, A
- CIT · Citric acid · additive · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.69 | 0.82 | 49 | empty |
| 2 | 449 | 0.68 | 0.79 | 65 | empty |
| 3 | 152 | 0.47 | 0.77 | 26 | empty |
| 4 | 157 | 0.45 | 0.75 | 26 | empty |
| 5 | 83 | 0.41 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- B–A · 596 Ų buried · 8 hydrogen bonds · protein-protein
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 O95255
- Elsewhere: RCSB PDB 6BZR · PDBe 6BZR · UniProt O95255
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