Research workbench
Crystal structure analysis of the ABC transporter from thermotoga maritima
Analyse Crystal structure analysis of the ABC transporter from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JI0
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter
- UniProt
- Q9X0M3
- Ligands
- ATP
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter | protein | 240 | 36% helix, 28% strand | Q9X0M3 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.51 | 0.76 | 30 | empty |
| 2 | 63 | 0.38 | 0.79 | 14 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 1JI0 · Crystal Structure Analysis of the ABC transporter from Thermotoga maritima · 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 Q9X0M3
- Elsewhere: RCSB PDB 1JI0 · PDBe 1JI0 · UniProt Q9X0M3
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