Research workbench
Crystal structure of the accessory translocation ATPase, SECA2, from clostridium difficile, in complex with adenosine-5'-(gamma-thio)- triphosphate
Analyse Crystal structure of the accessory translocation ATPase, SECA2, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T4H
- Type
- protein
- Length
- 771 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein translocase subunit seca 2
- UniProt
- Q183M9
- Ligands
- AGS
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca 2 | protein | 771 | 56% helix, 11% strand | Q183M9 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 934 | 0.79 | 0.82 | 86 | empty |
| 2 | 648 | 0.73 | 0.80 | 82 | AGS |
| 3 | 109 | 0.53 | 0.83 | 15 | empty |
| 4 | 73 | 0.53 | 0.85 | 16 | empty |
| 5 | 132 | 0.41 | 0.75 | 18 | empty |
Compared structures
- 6T4H · Crystal structure of the accessory translocation ATPase, SecA2, from Clostridium… · the same entry in another collection · chain A against A, TM-score 1.00
- Q183M9 · AlphaFold monomer V2.0 prediction for protein translocase subunit seca 2 (Q183M9) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q183M9
- Elsewhere: RCSB PDB 6T4H · PDBe 6T4H · UniProt Q183M9
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