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Crystal structure of an archease, possible chaperone (TM1083) from thermotoga maritima at 2.0 a resolution
Analyse Crystal structure of an archease, possible chaperone (TM1083) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J5U
- Type
- protein
- Length
- 127 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Archease, possible chaperone
- UniProt
- Q9X0H1
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Archease, possible chaperone | protein | 127 | 25% helix, 42% strand | Q9X0H1 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 1J5U · Crystal structure of an archease, possible chaperone (TM1083) from thermotoga maritima at… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X0H1 · AlphaFold monomer V2.0 prediction for protein archease (Q9X0H1) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q9X0H1
- Elsewhere: RCSB PDB 1J5U · PDBe 1J5U · UniProt Q9X0H1
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