Research workbench
Human ABCC6 NBD1 H812A in Apo state
Analyse Human ABCC6 NBD1 H812A in Apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NLO
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.85022
- Source
- Homo sapiens
- Molecule
- Multidrug resistance-associated protein 6
- UniProt
- O95255
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · resolution 2.85022 · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug resistance-associated protein 6 | protein | 227 | 32% helix, 27% strand | O95255 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.41 | 0.81 | 19 | empty |
| 2 | 79 | 0.37 | 0.76 | 17 | 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 O95255
- Elsewhere: RCSB PDB 6NLO · PDBe 6NLO · UniProt O95255
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