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Crystal structure of the translocation ATPase seca from thermus thermophilus reveals a parallel, head-to-head dimer
Analyse Crystal structure of the translocation ATPase seca from thermus thermophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IPC
- Type
- protein
- Length
- 3,746 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Preprotein translocase seca subunit
- UniProt
- Q5SIW3
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Preprotein translocase seca subunit | protein | 939 | 58% helix, 8% strand | Q5SIW3 |
| B, D | Preprotein translocase seca subunit | protein | 934 | 57% helix, 8% strand | Q5SIW3 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1064 | 0.86 | 0.87 | 116 | empty |
| 2 | 1115 | 0.81 | 0.82 | 103 | empty |
| 3 | 1108 | 0.81 | 0.82 | 98 | empty |
| 4 | 608 | 0.81 | 0.86 | 88 | empty |
| 5 | 972 | 0.80 | 0.82 | 68 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1799 Ų buried · 35 hydrogen bonds · protein-protein
- A–B · 1795 Ų buried · 37 hydrogen bonds · protein-protein
- A–D · 295 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2IPC · Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SIW3 · AlphaFold monomer V2.0 prediction for protein translocase subunit seca (Q5SIW3) · a predicted model of the same protein · chain B 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 Q5SIW3
- Elsewhere: RCSB PDB 2IPC · PDBe 2IPC · UniProt Q5SIW3
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