Research workbench
Crystal structure of SECA:ADP in an open conformation from bacillus subtilis
Analyse Crystal structure of SECA:ADP in an open conformation from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TF2
- Type
- protein
- Length
- 772 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Preprotein translocase seca subunit
- UniProt
- P28366
- Ligands
- ADP, MG
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Preprotein translocase seca subunit | protein | 772 | 53% helix, 12% strand | P28366 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 413 | 0.71 | 0.82 | 65 | MG, ADP |
| 2 | 258 | 0.61 | 0.80 | 39 | empty |
| 3 | 50 | 0.59 | 0.92 | 20 | empty |
| 4 | 243 | 0.56 | 0.77 | 25 | empty |
| 5 | 134 | 0.49 | 0.78 | 18 | empty |
Compared structures
- 1TF2 · Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis · the same entry in another collection · chain A against A, TM-score 1.00
- P28366 · AlphaFold monomer V2.0 prediction for protein translocase subunit seca (P28366) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 P28366
- Elsewhere: RCSB PDB 1TF2 · PDBe 1TF2 · UniProt P28366
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