Research workbench
Conformational changes of the clamp of the protein translocation ATPase seca from thermotoga maritima
Analyse Conformational changes of the clamp of the protein translocation ATPase seca… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YS0
- Type
- protein
- Length
- 814 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9X1R4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 814 | — | Q9X1R4 |
Compared structures
- 4YS0 · Conformational changes of the clamp of the protein translocation ATPase SecA from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X1R4 · AlphaFold monomer V2.0 prediction for protein translocase subunit seca (Q9X1R4) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9X1R4
- Elsewhere: RCSB PDB 4YS0 · PDBe 4YS0 · UniProt Q9X1R4
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