Research workbench
Crystal structure of ABC transporter ATP-binding protein (TM0544) from thermotoga maritima at 2.10 a resolution
Analyse Crystal structure of ABC transporter ATP-binding protein (TM0544) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VPL
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, ATP-binding protein
- UniProt
- Q9WZ14
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter, ATP-binding protein | protein | 238 | 41% helix, 27% strand | Q9WZ14 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.38 | 0.76 | 15 | empty |
Compared structures
- 1VPL · Crystal structure of ABC transporter ATP-binding protein (TM0544) from Thermotoga… · the same entry in another collection · chain A against A, 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 Q9WZ14
- Elsewhere: RCSB PDB 1VPL · PDBe 1VPL · UniProt Q9WZ14
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.